1n1m: Difference between revisions
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[[Image:1n1m.jpg|left|200px]] | [[Image:1n1m.jpg|left|200px]] | ||
'''Human Dipeptidyl Peptidase IV/CD26 in complex with an inhibitor''' | {{Structure | ||
|PDB= 1n1m |SIZE=350|CAPTION= <scene name='initialview01'>1n1m</scene>, resolution 2.50Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> and <scene name='pdbligand=A3M:2-AMINO-3-METHYL-1-PYRROLIDIN-1-YL-BUTAN-1-ONE'>A3M</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] | |||
|GENE= | |||
}} | |||
'''Human Dipeptidyl Peptidase IV/CD26 in complex with an inhibitor''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1N1M is a [ | 1N1M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1M OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12483204 12483204] | ||
[[Category: Dipeptidyl-peptidase IV]] | [[Category: Dipeptidyl-peptidase IV]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: dimer]] | [[Category: dimer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:50:54 2008'' | ||
Revision as of 13:50, 20 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Dipeptidyl-peptidase IV, with EC number 3.4.14.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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