| General information | | DisProt: | DP00355 | | Name: | Apolipoprotein E | | Synonym(s): | APOE_HUMAN
Apo-E
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P02649 | | UniGene: | Hs.654439 | | SwissProt: | APOE_HUMAN | | TrEMBL: | | | NCBI (GI): | 114039 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 317 | | Percent disordered: | 16% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MKVLWAALLV TFLAGCQAKV EQAVETEPEP ELRQQTEWQS GQRWELALGR FWDYLRWVQT - 60
LSEQVQEELL SSQVTQELRA LMDETMKELK AYKSELEEQL TPVAEETRAR LSKELQAAQA - 120
RLGADMEDVC GRLVQYRGEV QAMLGQSTEE LRVRLASHLR KLRKRLLRDA DDLQKRLAVY - 180
QAGAREGAER GLSAIRERLG PLVEQGRVRA ATVGSLAGQP LQERAQAWGE RLRARMEEMG - 240
SRTRDRLDEV KEQVAEVRAK LEEQAQQIRL QAEAFQARLK SWFEPLVEDM QRQWAGLVEK - 300
VQAAVGTSAA PVPSDNH
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| Functional narrative |
Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 19 - 39 | | Length: | 21 | | Region sequence: |
KVEQAVETEPEPELRQQTEWQ | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (pH: 5.6; PEG 400 (20-25%); Sodium cacodylate 50 mM)
- X-ray crystallography (pH: 5.6; Beta-mercaptoethanol (1%); PEG 400 (20-25%); Sodium cacodylate 50 mM)
- X-ray crystallography (pH: 5.6; PEG 400 (15-20%); Sodium cacodylate 50 mM)
| References:
- Segelke BW, Forstner M, Knapp M, Trakhanov SD, Parkin S, Newhouse YM, Bellamy HD, Weisgraber KH, Rupp B. "Conformational flexibility in the apolipoprotein E amino-terminal domain structure determined from three new crystal forms: implications for lipid binding." Protein Sci. 2000; 9(5): 886-97. PubMed: 10850798
- Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA. "Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E." Science. 1991; 252(5014): 1817-22. PubMed: 2063194
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | 80s Loop | | Location: | 100 - 104 | | Length: | 5 | | Region sequence: |
LTPVA | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-lipid interaction
| Detection methods:
- X-ray crystallography (Beta-mercaptoethanol (0.1%); Beta-n-octylglucopyranoside (0.2%); PEG 400 (15%); Sodium acetate-acetic acid buffer 20 mM)
- X-ray crystallography (pH: 5.6; PEG 400 (20-25%); Sodium cacodylate 50 mM)
- X-ray crystallography (pH: 5.6; Beta-mercaptoethanol (1%); PEG 400 (20-25%); Sodium cacodylate 50 mM)
- X-ray crystallography (pH: 5.6; PEG 400 (15-20%); Sodium cacodylate 50 mM)
| References:
- Segelke BW, Forstner M, Knapp M, Trakhanov SD, Parkin S, Newhouse YM, Bellamy HD, Weisgraber KH, Rupp B. "Conformational flexibility in the apolipoprotein E amino-terminal domain structure determined from three new crystal forms: implications for lipid binding." Protein Sci. 2000; 9(5): 886-97. PubMed: 10850798
- Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA. "Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E." Science. 1991; 252(5014): 1817-22. PubMed: 2063194
| Comments:
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| Region 3 | | Type: | Disordered | | Name: | | | Location: | 185 - 209 | | Length: | 25 | | Region sequence: |
REGAERGLSAIRERLGPLVEQGRVR | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (Beta-mercaptoethanol (0.1%); Beta-n-octylglucopyranoside (0.2%); PEG 400 (15%); protein 10 mg/ml; Sodium acetate-acetic acid buffer 20 mM)
| References:
- Segelke BW, Forstner M, Knapp M, Trakhanov SD, Parkin S, Newhouse YM, Bellamy HD, Weisgraber KH, Rupp B. "Conformational flexibility in the apolipoprotein E amino-terminal domain structure determined from three new crystal forms: implications for lipid binding." Protein Sci. 2000; 9(5): 886-97. PubMed: 10850798
- Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA. "Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E." Science. 1991; 252(5014): 1817-22. PubMed: 2063194
| Comments:
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| References |
- Rall SC Jr, Weisgraber KH, Mahley RW. "Human apolipoprotein E. The complete amino acid sequence." J Biol Chem. 1982; 257(8): 4171-8. PubMed: 7068630
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| Comments |
The fragements used to determine the crystal structure did not include the first 18 residues of the precursor sequence.
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