Basic Pancreatic Trypsin Inhibitor
From Proteopedia
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- | + | <StructureSection load='3tgi' size='350' side='right' scene='43/430026/Cv/2' caption='Bovine BPTI (in salmon) complex with trypsin (magenta), sulfate and Ca+2 ion (green) (PDB code [[3tgi]])'> | |
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- | + | == Function == | |
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- | + | [[Basic Pancreatic Trypsin Inhibitor]] (BPTI) is a small protein which inhibits trypsin and related proteases. <ref>PMID:15299722</ref> For other trypsin inhibitors see [[Trypsin inhibitor]]. | |
- | == | + | == Relevance == |
- | + | BPTI is used as drug called Aprotinin used to reduce bleeding during surgery. | |
- | + | == Structural highlights == | |
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+ | <scene name='43/430026/Cv/3'>Residue K15 of BPTI</scene> extends into the active site of trypsin and inhibits its proteolytic function. <ref>PMID:10210204</ref> | ||
+ | == 3D Structures of BPTI == | ||
+ | [[BPTI 3D structures]] | ||
- | + | </StructureSection> | |
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+ | == References == | ||
+ | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Current revision
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References
- ↑ Parkin S, Rupp B, Hope H. Structure of bovine pancreatic trypsin inhibitor at 125 K definition of carboxyl-terminal residues Gly57 and Ala58. Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):18-29. PMID:15299722 doi:http://dx.doi.org/10.1107/S0907444995008675
- ↑ Pasternak A, Ringe D, Hedstrom L. Comparison of anionic and cationic trypsinogens: the anionic activation domain is more flexible in solution and differs in its mode of BPTI binding in the crystal structure. Protein Sci. 1999 Jan;8(1):253-8. PMID:10210204