1n1m: Difference between revisions
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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 15:01, 21 February 2008
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Human Dipeptidyl Peptidase IV/CD26 in complex with an inhibitor
OverviewOverview
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 StructureAbout 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.
ReferenceReference
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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