1NU6

Crystal structure of human Dipeptidyl Peptidase IV (DPP-IV)

1NU6 の概要

• エントリーDOI: 10.2210/pdb1nu6/pdb
• 関連するPDBエントリー: 1NU8
• 分子名称: Dipeptidyl peptidase IV, 2-acetamido-2-deoxy-beta-D-glucopyranose, MERCURY (II) ION, ... (4 entities in total)
• 機能のキーワード: exopeptidase, beta barrel, alpha/beta hydrolase fold, dpp-iv, 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: 171898.44

構造登録者

Hennig, M.,Stihle, M.,Thoma, R.,Ruf, A. (登録日: 2003-01-31, 公開日: 2003-08-26, 最終更新日: 2024-11-13)

主引用文献

Thoma, R.,Loeffler, B.,Stihle, M.,Huber, W.,Ruf, A.,Hennig, M.
Structural Basis of Proline-Specific Exopeptidase Activity as Observed in Human Dipeptidyl Peptidase-IV.
Structure, 11:947-959, 2003

PubMed Abstract: Inhibition of dipeptidyl peptidase IV (DPP-IV), the main glucagon-like peptide 1 (GLP1)-degrading enzyme, has been proposed for the treatment of type II diabetes. We expressed and purified the ectodomain of human DPP-IV in Pichia pastoris and determined the X-ray structure at 2.1 A resolution. The enzyme consists of two domains, the catalytic domain, with an alpha/beta hydrolase fold, and a beta propeller domain with an 8-fold repeat of a four-strand beta sheet motif. The beta propeller domain contributes two important functions to the molecule that have not been reported for such structures, an extra beta sheet motif that forms part of the dimerization interface and an additional short helix with a double Glu sequence motif. The Glu motif provides recognition and a binding site for the N terminus of the substrates, as revealed by the complex structure with diprotin A, a substrate with low turnover that is trapped in the tetrahedral intermediate of the reaction in the crystal.

PubMed: 12906826
DOI: 10.1016/S0969-2126(03)00160-6

実験手法

X-RAY DIFFRACTION (2.1 Å)