Basic Pancreatic Trypsin Inhibitor
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
| - | <scene name='43/430026/Cv/3'>Residue K15 of BPTI</scene> extends into the active site of trypsin and inhibits its proteolytic function. | + | <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> |
</StructureSection> | </StructureSection> | ||
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**[[4bnr]] - bBPTI+ hepatopancreas trypsin<br /> | **[[4bnr]] - bBPTI+ hepatopancreas trypsin<br /> | ||
}} | }} | ||
| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 13:22, 15 November 2015
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3D Structures of BPTI
Updated on 15-November-2015
References
- ↑ 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
