1n1m
From Proteopedia
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'''Human Dipeptidyl Peptidase IV/CD26 in complex with an inhibitor''' | '''Human Dipeptidyl Peptidase IV/CD26 in complex with an inhibitor''' | ||
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[[Category: Wagtmann, N R.]] | [[Category: Wagtmann, N R.]] | ||
[[Category: Wiberg, F C.]] | [[Category: Wiberg, F C.]] | ||
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- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:58:36 2008'' | |
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Revision as of 22:58, 2 May 2008
Human Dipeptidyl Peptidase IV/CD26 in complex with an inhibitor
Overview
Dipeptidyl peptidase IV (DPP-IV/CD26) is a multifunctional type II transmembrane serine peptidase. This enzyme contributes to the regulation of various physiological processes, including blood sugar homeostasis, by cleaving peptide hormones, chemokines and neuropeptides. We have determined the 2.5 A structure of the extracellular region of DPP-IV in complex with the inhibitor valine-pyrrolidide. The catalytic site is located in a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain. Both domains participate in inhibitor binding. The structure indicates how substrate specificity is achieved and reveals a new and unexpected opening to the active site.
About this Structure
1N1M is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog., Rasmussen HB, Branner S, Wiberg FC, Wagtmann N, Nat Struct Biol. 2003 Jan;10(1):19-25. PMID:12483204 Page seeded by OCA on Sat May 3 01:58:36 2008