FSGSEATAAILSRAPWSLQSVNPGLKTNSSKE

1. X-ray crystallography (1:1 complex (structure determined at 2.6 Angstroms); 1:2 complex (structure determined at 2.6 Angstroms))

1. Clackson T, Ultsch MH, Wells JA, de Vos AM. "Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity." J Mol Biol. 1998; 277(5): 1111-28. PubMed: 9571026
   
   

DEVHHGTKN

1. X-ray crystallography (1:1 complex (structure determined at 2.6 Angstroms); 1:2 complex (structure determined at 2.6 Angstroms))

1. Clackson T, Ultsch MH, Wells JA, de Vos AM. "Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity." J Mol Biol. 1998; 277(5): 1111-28. PubMed: 9571026
   
   

VSLT

1. X-ray crystallography (1:1 complex (structure determined at 2.6 Angstroms); 1:2 complex (structure determined at 2.6 Angstroms))

1. Clackson T, Ultsch MH, Wells JA, de Vos AM. "Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity." J Mol Biol. 1998; 277(5): 1111-28. PubMed: 9571026
   
   

Q

1. X-ray crystallography (1:1 complex (structure determined at 2.6 Angstroms); 1:2 complex (structure determined at 2.6 Angstroms))

1. Clackson T, Ultsch MH, Wells JA, de Vos AM. "Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity." J Mol Biol. 1998; 277(5): 1111-28. PubMed: 9571026
   
   

YGEFS

1. X-ray crystallography (1:1 complex (structure determined at 2.6 Angstroms); 1:2 complex (structure determined at 2.6 Angstroms))


2. X-ray crystallography (pH: 5.5; 1:2 complex (structure determined at 2.8 Angstroms); K2AuCl4; K2PtCl4; saturated ammonium sulfate 40 %; sodium acetate 0.1 M)

1. Clackson T, Ultsch MH, Wells JA, de Vos AM. "Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity." J Mol Biol. 1998; 277(5): 1111-28. PubMed: 9571026
   
   
2. de Vos AM, Ultsch M, Kossiakoff AA. "Human growth hormone and extracellular domain of its receptor: crystal structure of the complex." Science. 1992; 255(5042): 306-312. PubMed: 1549776
   
   

Residues 222-226 had poor electron density and were not modeled in the crystal structure (Clackson, 1998).

TQEWTQ

1. X-ray crystallography (1:1 complex (structure determined at 2.6 Angstroms); 1:2 complex (structure determined at 2.6 Angstroms))


2. X-ray crystallography (pH: 5.5; 1:2 complex (structure determined at 2.8 Angstroms); K2AuCl4; K2PtCl4; saturated ammonium sulfate 40 %; sodium acetate 0.1 M)

1. Clackson T, Ultsch MH, Wells JA, de Vos AM. "Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity." J Mol Biol. 1998; 277(5): 1111-28. PubMed: 9571026
   
   
2. de Vos AM, Ultsch M, Kossiakoff AA. "Human growth hormone and extracellular domain of its receptor: crystal structure of the complex." Science. 1992; 255(5042): 306-312. PubMed: 1549776
   
   

The binding proteins of the 1:2 (hormone:binding protein) complex are hGHbp I and hGHbp II. De Vos found this region to be disordered in hGHbp I (de Vos 1992).

FSGSEATAAILSRAPWSLQSVNPGLKTNSSK

1. X-ray crystallography (291 K; 1:1 complex (crystals defracted to 2.9 Angstroms); 1:2 complex (crystals defracted to 2.5 Angstroms); 50% saturated LiSO4 solution (to stabilize); Bis-Tris (pH 6.25-6.75) 50 mM; LiSO4 (3 microliters) 1.6 M; MES (pH 5.25 (to stabilize)) 0.1 M; MgCl2 (to stabilize) 0.5 mM)

1. Sundstrom M, Lundqvist T, Rodin J, Giebel LB, Milligan D, Norstedt G. "Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9 A resolution." J Biol Chem. 1996; 271(50): 32197-32203. PubMed: 8943276
   
   

The N-terminus region of the hGHbp, for both the native 1:2 complex and the mutated 1:1 complex, had missing electron density for the first 31 residues (Sundstrom, 1996).

WTDEVHHGTKNLG

1. X-ray crystallography (291 K; 1:1 complex (crystals defracted to 2.9 Angstroms); 1:2 complex (crystals defracted to 2.5 Angstroms); 50% saturated LiSO4 solution (to stabilize); Bis-Tris (pH 6.25-6.75) 50 mM; LiSO4 (3 microliters) 1.6 M; MES (pH 5.25 (to stabilize) ) 0.1 M; MgCl2 (to stabilize) 0.5 mM)

1. Sundstrom M, Lundqvist T, Rodin J, Giebel LB, Milligan D, Norstedt G. "Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9 A resolution." J Biol Chem. 1996; 271(50): 32197-32203. PubMed: 8943276
   
   

NTQEWTQ

1. X-ray crystallography (291 K; 1:1 complex (crystals defracted to 2.9 Angstroms); 1:2 complex (crystals defracted to 2.5 Angstroms); 50% saturated LiSO4 solution (to stabilize); Bis-Tris (pH 6.25-6.75) 50 mM; LiSO4 (3 microliters) 1.6 M; MES (pH 5.25 (to stabilize)) 0.1 M; MgCl2 (to stabilize ) 0.5 mM)

1. Sundstrom M, Lundqvist T, Rodin J, Giebel LB, Milligan D, Norstedt G. "Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9 A resolution." J Biol Chem. 1996; 271(50): 32197-32203. PubMed: 8943276
   
   

PQMS

1. X-ray crystallography (291 K; 1:1 complex (crystals defracted to 2.9 Angstroms); 1:2 complex (crystals defracted to 2.5 Angstroms); 50% saturated LiSO4 solution (to stabilize); Bis-Tris (pH 6.25-6.75) 50 mM; LiSO4 (3 microliters) 1.6 M; MES (pH 5.25 (to stabilize)) 0.1 M; MgCl2 (to stabilize) 0.5 mM)

1. Sundstrom M, Lundqvist T, Rodin J, Giebel LB, Milligan D, Norstedt G. "Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9 A resolution." J Biol Chem. 1996; 271(50): 32197-32203. PubMed: 8943276
   
   

FSGSE

1. X-ray crystallography (1:1 complex (structure determined at 2.6 Angstroms); 1:2 complex (structure determined at 2.6 Angstroms))

1. Clackson T, Ultsch MH, Wells JA, de Vos AM. "Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity." J Mol Biol. 1998; 277(5): 1111-28. PubMed: 9571026
   
   

VSLTG

1. X-ray crystallography (1:1 complex (structure determined at 2.6 Angstroms); 1:2 complex (structure determined at 2.6 Angstroms))

1. Clackson T, Ultsch MH, Wells JA, de Vos AM. "Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity." J Mol Biol. 1998; 277(5): 1111-28. PubMed: 9571026
   
   

This region is likely stabilized upon binding of the second receptor to the growth hormone in the 1:2 complex (Clackson, 1998).

FSGSEATAAILSRAPWSLQSVNPGLKTNSS

1. X-ray crystallography (pH: 5.5; 1:2 complex (structure determined at 2.8 Angstroms); K2AuCl4; K2PtCl4; saturated ammonium sulfate 40 %; sodium acetate 0.1 M)

1. de Vos AM, Ultsch M, Kossiakoff AA. "Human growth hormone and extracellular domain of its receptor: crystal structure of the complex." Science. 1992; 255(5042): 306-312. PubMed: 1549776
   
   

The binding proteins of the 1:2 (hormone:binding protein) complex are hGHbp I and hGHbp II. De Vos found this region to be disordered in hGHbp II (de Vos 1992).

VHHGTKN

1. X-ray crystallography (pH: 5.5; 1:2 complex (structure determined at 2.8 Angstroms); K2AuCl4; K2PtCl4; saturated ammonium sulfate 40 %; sodium acetate 0.1 M)

1. de Vos AM, Ultsch M, Kossiakoff AA. "Human growth hormone and extracellular domain of its receptor: crystal structure of the complex." Science. 1992; 255(5042): 306-312. PubMed: 1549776
   
   

The binding proteins of the 1:2 (hormone:binding protein) complex are hGHbp I and hGHbp II. De Vos found this region to be disordered in hGHbp II (de Vos 1992).

TQE

1. X-ray crystallography (pH: 5.5; 1:2 complex (structure determined at 2.8 Angstroms); K2AuCl4; K2PtCl4; saturated ammonium sulfate 40 %; sodium acetate 0.1 M)

1. de Vos AM, Ultsch M, Kossiakoff AA. "Human growth hormone and extracellular domain of its receptor: crystal structure of the complex." Science. 1992; 255(5042): 306-312. PubMed: 1549776
   
   

In the de Vos reference, (de Vos_Science_255_306-312), they refer to both of the binding proteins of the 1:2 (hormone:binding proteins) complex. They are named hGHbp I and hGHbp II. De Vos found this region to be disordered in the hGHbp II.

FSGSEATAAILSRAPWSLQSVNPGLKTN

1. X-ray crystallography (pH: 5.5; 1:2 complex (structure determined at 2.8 Angstroms); K2AuCl4; K2PtCl4; saturated ammonium sulfate 40 %; sodium acetate 0.1 M)

1. de Vos AM, Ultsch M, Kossiakoff AA. "Human growth hormone and extracellular domain of its receptor: crystal structure of the complex." Science. 1992; 255(5042): 306-312. PubMed: 1549776
   
   

In the de Vos reference, (de Vos_Science_255_306-312), they refer to both of the binding proteins of the 1:2 (hormone:binding proteins) complex. They are named hGHbp I and hGHbp II. De Vos found this region to be disordered in the hGHbp I.

HHGT

1. X-ray crystallography (pH: 5.5; 1:2 complex (structure determined at 2.8 Angstroms); K2AuCl4; K2PtCl4; saturated ammonium sulfate 40 %; sodium acetate 0.1 M)

1. de Vos AM, Ultsch M, Kossiakoff AA. "Human growth hormone and extracellular domain of its receptor: crystal structure of the complex." Science. 1992; 255(5042): 306-312. PubMed: 1549776
   
   

The binding proteins of the 1:2 (hormone:binding protein) complex are hGHbp I and hGHbp II. De Vos found this region to be disordered in hGHbp I (de Vos 1992).

QMSQ

1. X-ray crystallography (pH: 5.5; 1:2 complex (structure determined at 2.8 Angstroms); K2AuCl4 ; K2PtCl4; saturated ammonium sulfate 40 %; sodium acetate 0.1 M)

1. de Vos AM, Ultsch M, Kossiakoff AA. "Human growth hormone and extracellular domain of its receptor: crystal structure of the complex." Science. 1992; 255(5042): 306-312. PubMed: 1549776
   
   

The binding proteins of the 1:2 (hormone:binding protein) complex are hGHbp I and hGHbp II. De Vos found this region to be disordered in hGHbp I (de Vos 1992).

1. Clackson T, Ultsch MH, Wells JA, de Vos AM. "Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity." J Mol Biol. 1998; 277(5): 1111-28. PubMed: 9571026
   
   
2. Clackson T, Wells JA. "A hot spot of binding energy in a hormone-receptor interface." Science. 1995; 267(5196): 383-6. PubMed: 7529940
   
   
3. de Vos AM, Ultsch M, Kossiakoff AA. "Human growth hormone and extracellular domain of its receptor: crystal structure of the complex." Science. 1992; 255(5042): 306-312. PubMed: 1549776
   
   
4. Fuh G, Mulkerrin MG, Bass S, McFarland N, Brochier M, Bourell JH, Light DR, Wells JA. "The human growth hormone receptor. Secretion from Escherichia coli and disulfide bonding pattern of the extracellular binding domain." J Biol Chem. 1990; 265(6): 3111-3115. PubMed: 2406245
   
   
5. Sundstrom M, Lundqvist T, Rodin J, Giebel LB, Milligan D, Norstedt G. "Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9 A resolution." J Biol Chem. 1996; 271(50): 32197-32203. PubMed: 8943276
   
   

Human Growth Hormone binding protein (hGHbp) exists as a fully functional 238 residue protein in serum. These 238 residues are a fragment of a larger protein, human Growth Hormone Receptor, (hGH receptor), which has 638 residues. hGH consists of three domains; an extracellular binding domain- located outside of the membrane, a transmembrane domain, and a cytosolic domain. “It has been proposed that the hGH binding protein in serum derives from proteolysis of the membrane-bound form of the receptor near the transmembrane anchor" (Fuh, 1990).

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Residues 73-78 were not modeled in the crystal structure due to poor electron density (Clackson, 1998).

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There is some disagreement about the whether the protein is 238 residues long, as it is when attached to the entire hGH receptor, or if it is 246 residues long, as it is when it is found freely in serum. However, the nine residue segment was shown to be not essential for function (Fuh, 1990).

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The UniProt entry for this protein mentions that one isoform has a different function: upregulation of the production of GHBP and as a negative inhibitor of GH signaling.

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The SwissProt entry states that the first 18 residues of the amino acid sequence form a signal sequence and are not considered part of the extracellular binding domain. Therefore, the extracellular binding domain starts at residue 19 and extends through residue 264. This sequence is 246 residues long.

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One human growth hormone binding protein (hGHbp) binds to a human growth hormone (hGH) followed by the binding of a second hGHbp to the same hGH. After the second hGHbp binds the two hGHbps (I and II) dimerize.

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Additional UniGene ID, Hs.684631

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Previous entry DP00033 has been split into polyprotein DP00033 and cleavage product DP00033_C001. Disorder is characterized on the cleavage product.