Rasmussen_2003_Nat.Struct.Biol_10_19

Reference

Title : Crystal structure of human dipeptidyl peptidase IV\/CD26 in complex with a substrate analog - Rasmussen_2003_Nat.Struct.Biol_10_19
Author(s) : Rasmussen HB , Branner S , Wiberg FC , Wagtmann N
Ref : Nat Struct Biol , 10 :19 , 2003
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.
ESTHER : Rasmussen_2003_Nat.Struct.Biol_10_19
PubMedSearch : Rasmussen_2003_Nat.Struct.Biol_10_19
PubMedID: 12483204
Gene_locus related to this paper: human-DPP4

Related information

Gene_locus related to this paper: human-DPP4

Citations formats

Rasmussen HB, Branner S, Wiberg FC, Wagtmann N (2003)
Crystal structure of human dipeptidyl peptidase IV\/CD26 in complex with a substrate analog
Nat Struct Biol 10 :19

Rasmussen HB, Branner S, Wiberg FC, Wagtmann N (2003)
Nat Struct Biol 10 :19