1w1i

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[[Category: serine protease]]
[[Category: serine protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:56:36 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:21:44 2007''

Revision as of 14:17, 30 October 2007


1w1i, resolution 3.03Å

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CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV (DPPIV OR CD26) IN COMPLEX WITH ADENOSINE DEAMINASE

Overview

Dipeptidyl-peptidase IV (DPPIV or CD26) is a homodimeric type II membrane, glycoprotein in which the two monomers are subdivided into a, beta-propeller domain and an alpha/beta-hydrolase domain. As dipeptidase, DPPIV modulates the activity of various biologically important peptides, and, in addition, DPPIV acts as a receptor for adenosine deaminase (ADA), thereby mediating co-stimulatory signals in T-lymphocytes. The 3.0-A, resolution crystal structure of the complex formed between human DPPIV and, bovine ADA presented here shows that each beta-propeller domain of the, DPPIV dimer binds one ADA. At the binding interface, two hydrophobic loops, protruding from the beta-propeller domain of DPPIV interact with two, hydrophilic and heavily charged alpha-helices of ADA, giving rise to the, ... [(full description)]

About this Structure

1W1I is a [Protein complex] structure of sequences from [Bos taurus] and [Homo sapiens] with NAG, NDG and ZN as [ligands]. Active as [Dipeptidyl-peptidase IV], with EC number [3.4.14.5]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structure of CD26/dipeptidyl-peptidase IV in complex with adenosine deaminase reveals a highly amphiphilic interface., Weihofen WA, Liu J, Reutter W, Saenger W, Fan H, J Biol Chem. 2004 Oct 8;279(41):43330-5. Epub 2004 Jun 22. PMID:15213224

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