1w1i
From Proteopedia
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==Overview== | ==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, ... | + | 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, highest percentage of charged residues involved in a protein-protein, contact reported thus far. Additionally, four glycosides linked to Asn229, of DPPIV bind to ADA. In the crystal structure of porcine DPPIV, the, observed tetramer formation was suggested to mediate epithelial and, lymphocyte cell-cell adhesion. ADA binding to DPPIV could regulate this, adhesion, as it would abolish tetramerization. |
==About this Structure== | ==About this Structure== | ||
| - | 1W1I is a | + | 1W1I is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG, NDG and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W1I OCA]. |
==Reference== | ==Reference== | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:20:39 2007'' |
Revision as of 12:15, 5 November 2007
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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, highest percentage of charged residues involved in a protein-protein, contact reported thus far. Additionally, four glycosides linked to Asn229, of DPPIV bind to ADA. In the crystal structure of porcine DPPIV, the, observed tetramer formation was suggested to mediate epithelial and, lymphocyte cell-cell adhesion. ADA binding to DPPIV could regulate this, adhesion, as it would abolish tetramerization.
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
Page seeded by OCA on Mon Nov 5 14:20:39 2007
Categories: Bos taurus | Dipeptidyl-peptidase IV | Homo sapiens | Protein complex | Fan, H. | Liu, J. | Reutter, W. | Saenger, W. | Weihofen, W.A. | NAG | NDG | ZN | Ada | Adenosine deaminase | Alpha/beta-hydrolase fold | Aminopeptidase | Beta-propeller fold | Cd26 | Dipetidyl peptidase iv | Dppiv | Protein-protein complex | Serine protease
