1n1m
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Dipeptidyl peptidase IV (DPP-IV/CD26) is a multifunctional type II | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Branner, S.]] | [[Category: Branner, S.]] | ||
| - | [[Category: Rasmussen, H | + | [[Category: Rasmussen, H B.]] |
| - | [[Category: Wagtmann, N | + | [[Category: Wagtmann, N R.]] |
| - | [[Category: Wiberg, F | + | [[Category: Wiberg, F C.]] |
[[Category: A3M]] | [[Category: A3M]] | ||
[[Category: HG]] | [[Category: HG]] | ||
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[[Category: dimer]] | [[Category: dimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:20 2008'' |
Revision as of 12:01, 21 February 2008
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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 , and 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
Page seeded by OCA on Thu Feb 21 14:01:20 2008
Categories: Dipeptidyl-peptidase IV | Homo sapiens | Single protein | Branner, S. | Rasmussen, H B. | Wagtmann, N R. | Wiberg, F C. | A3M | HG | NAG | Alpha/beta | Beta-propeller | Dimer
