1n1m

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(New page: 200px<br /> <applet load="1n1m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n1m, resolution 2.50&Aring;" /> '''Human Dipeptidyl Pe...)
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Revision as of 16:10, 12 November 2007

Image:1n1m.gif

1n1m, resolution 2.50Å

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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 with NAG, HG and A3M as ligands. Active as Dipeptidyl-peptidase IV, with EC number 3.4.14.5 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

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