General information | DisProt: | DP00729 | Name: | Pancreatic trypsin inhibitor | Synonym(s): | BPT1_BOVIN
Aprotinin
Basic protease inhibitor
BPTI
BPI
| First appeared in release: | Release 6.00 (07/01/2012) | UniProt: | P00974 | UniGene: | | SwissProt: | BPT1_BOVIN | TrEMBL: | | NCBI (GI): | | Source organism: | Bos taurus (Bovine) | Sequence length: | 100 | Percent disordered: | 34% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MKMSRLCLSV ALLVLLGTLA ASTPGCDTSN QAKAQRPDFC LEPPYTGPCK ARIIRYFYNA - 60 KAGLCQTFVY GGCRAKRNNF KSAEDCMRTC GGAIGPWENL
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Functional narrative |
Function: Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.
Subcellular Location: Secreted.
PHARMACEUTICAL: Available under the name Trasylol (Mile). Used for inhibiting coagulation so as to reduce blood loss during bypass surgery.
SIMILARITY: Contains 1 BPTI/Kunitz inhibitor domain.
WEB RESOURCE: Name=Trasylol; Note=Clinical information on Trasylol; URL='http://www.trasylol.com/';
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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: | L64 | Location: | 64 - 64 | Length: | 1 | Region sequence: |
L | Modification type: | Engineered
| PDB: | 1G6X:A | Structural/functional type: | Function arises from the disordered state | Functional classes: | | Functional subclasses: | Intraprotein interaction
| Detection methods:
- X-ray crystallography (292 K; pH: 7.5; BPTI protein 4.5 mg/uL; PEG 400 2 %; Ammonium sulfate 2 M; Na-HEPES 0.1 M; Ethylene glycol (cryoprotectant))
| References:
- Addlagatta A, Krzywda S, Czapinska H, Otlewski J, Jaskolski M. "Ultrahigh-resolution structure of a BPTI mutant." Acta Crystallogr. D Biol. Crystallogr.. 2001; 57(Pt 5): 649-63. PubMed: 11320305
| Comments:
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Region 2 | Type: | Disordered | Name: | auxiliary loop | Location: | 49 - 73 | Length: | 25 | Region sequence: |
CKARIIRYFYNAKAGLCQTFVYGGC | Modification type: | Engineered
| PDB: | 1G6X:A | Structural/functional type: | Function arises from the disordered state | Functional classes: | | Functional subclasses: | Intraprotein interaction
| Detection methods:
- X-ray crystallography (292 K; pH: 7.5; Ammonium sulfate 2 M; BPTI protein 4.5 mg/uL; Ethylene glycol (cryoprotectant); Na-HEPES 0.1 M; PEG 400 2 %)
| References:
- Addlagatta A, Krzywda S, Czapinska H, Otlewski J, Jaskolski M. "Ultrahigh-resolution structure of a BPTI mutant." Acta Crystallogr. D Biol. Crystallogr.. 2001; 57(Pt 5): 649-63. PubMed: 11320305
| Comments:Residues C49 and C73 form a disulfide bridge.
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Region 3 | Type: | Disordered | Name: | | Location: | 81 - 87 | Length: | 7 | Region sequence: |
KSAEDCM | Modification type: | Engineered
| PDB: | 1G6X:A | Structural/functional type: | Function arises from the disordered state | Functional classes: | | Functional subclasses: | Intraprotein interaction
| Detection methods:
- X-ray crystallography (292 K; pH: 7.5; Ammonium sulfate 2 M; BPTI protein 4.5 mg/uL; Ethylene glycol (cryoprotectant); Na-HEPES 0.1 M; PEG 400 2 %)
| References:
- Addlagatta A, Krzywda S, Czapinska H, Otlewski J, Jaskolski M. "Ultrahigh-resolution structure of a BPTI mutant." Acta Crystallogr. D Biol. Crystallogr.. 2001; 57(Pt 5): 649-63. PubMed: 11320305
| Comments:
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Region 4 | Type: | Disordered | Name: | disordered GG | Location: | 91 - 92 | Length: | 2 | Region sequence: |
GG | Modification type: | Engineered
| PDB: | 1G6X:A | Structural/functional type: | Function arises from the disordered state | Functional classes: | | Functional subclasses: | Intraprotein interaction
| Detection methods:
- X-ray crystallography (292 K; pH: 7.5; Ammonium sulfate 2 M; BPTI protein 4.5 mg/uL; Ethylene glycol (cryoprotectant); Na-HEPES 0.1 M; PEG 400 2 %)
| References:
- Addlagatta A, Krzywda S, Czapinska H, Otlewski J, Jaskolski M. "Ultrahigh-resolution structure of a BPTI mutant." Acta Crystallogr. D Biol. Crystallogr.. 2001; 57(Pt 5): 649-63. PubMed: 11320305
| Comments:
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Comments |
Addlagatta et al (2001) used mature BPTI (UniProt aa 36-93) engineered with the following mutations: T46A, P48A, K50R and M87L.
UniProt describes residue K50 as a "reactive bond for trypsin" and C40-C90 as "BPTI/Kunitz inhibitor" domain.
AV sent 6-26-2012 (PMID:11320305)
[AV received 6/26/12]
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