1N1M

Human Dipeptidyl Peptidase IV/CD26 in complex with an inhibitor

1N1M の概要

• エントリーDOI: 10.2210/pdb1n1m/pdb
• 分子名称: Dipeptidyl peptidase IV SOLUBLE FORM, MERCURY (II) ION, 2-AMINO-3-METHYL-1-PYRROLIDIN-1-YL-BUTAN-1-ONE, ... (12 entities in total)
• 機能のキーワード: alpha/beta, beta-propeller, dimer, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 176121.79

構造登録者

Rasmussen, H.B.,Branner, S.,Wiberg, F.C.,Wagtmann, N.R. (登録日: 2002-10-18, 公開日: 2002-12-27, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)