1n1m
From Proteopedia
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|PDB= 1n1m |SIZE=350|CAPTION= <scene name='initialview01'>1n1m</scene>, resolution 2.50Å | |PDB= 1n1m |SIZE=350|CAPTION= <scene name='initialview01'>1n1m</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=A3M:2-AMINO-3-METHYL-1-PYRROLIDIN-1-YL-BUTAN-1-ONE'>A3M</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n1m OCA], [http://www.ebi.ac.uk/pdbsum/1n1m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n1m RCSB]</span> | ||
}} | }} | ||
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[[Category: Wagtmann, N R.]] | [[Category: Wagtmann, N R.]] | ||
[[Category: Wiberg, F C.]] | [[Category: Wiberg, F C.]] | ||
| - | [[Category: A3M]] | ||
| - | [[Category: HG]] | ||
| - | [[Category: NAG]] | ||
[[Category: alpha/beta]] | [[Category: alpha/beta]] | ||
[[Category: beta-propeller]] | [[Category: beta-propeller]] | ||
[[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 Sun Mar 30 22:24:03 2008'' |
Revision as of 19:24, 30 March 2008
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , | ||||||
| Activity: | Dipeptidyl-peptidase IV, with EC number 3.4.14.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 22:24:03 2008
