1N1M

Human Dipeptidyl Peptidase IV/CD26 in complex with an inhibitor

Summary for 1N1M

• Entry DOI: 10.2210/pdb1n1m/pdb
• Descriptor: Dipeptidyl peptidase IV SOLUBLE FORM, MERCURY (II) ION, 2-AMINO-3-METHYL-1-PYRROLIDIN-1-YL-BUTAN-1-ONE, ... (12 entities in total)
• Functional Keywords: alpha/beta, beta-propeller, dimer, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 176121.79

Authors

Rasmussen, H.B.,Branner, S.,Wiberg, F.C.,Wagtmann, N.R. (deposition date: 2002-10-18, release date: 2002-12-27, Last modification date: 2024-10-30)

Primary citation

Rasmussen, H.B.,Branner, S.,Wiberg, F.C.,Wagtmann, N.R.
Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analogue
Nat.Struct.Biol., 10:19-25, 2003

PubMed Abstract: 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.

PubMed: 12483204
DOI: 10.1038/nsb882

Experimental method

X-RAY DIFFRACTION (2.5 Å)