1rct

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{{STRUCTURE_1rct| PDB=1rct | SCENE= }}
{{STRUCTURE_1rct| PDB=1rct | SCENE= }}
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'''Crystal structure of Human purine nucleoside phosphorylase complexed with INOSINE'''
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===Crystal structure of Human purine nucleoside phosphorylase complexed with INOSINE===
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==Overview==
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Human purine nucleoside phosphorylase (PNP) is a ubiquitous enzyme which plays a key role in the purine salvage pathway, and PNP deficiency in humans leads to an impairment of T-cell function, usually with no apparent effect on B-cell function. PNP is highly specific for 6-oxopurine nucleosides and exhibits negligible activity for 6-aminopurine nucleosides. The catalytic efficiency for inosine is 350,000-fold greater than for adenosine. Adenine nucleosides and nucleotides are deaminated by adenosine deaminase and AMP deaminase to their corresponding inosine derivatives which, in turn, may be further degraded. Here we report the crystal structures of human PNP in complex with inosine and 2('),3(')-dideoxyinosine, refined to 2.8A resolution using synchrotron radiation. The present structures provide explanation for ligand binding, refine the purine-binding site, and can be used for future inhibitor design.
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(as it appears on PubMed at http://www.pubmed.gov), where 14706628 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14706628}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structures of human purine nucleoside phosphorylase complexed with inosine and ddI., Canduri F, dos Santos DM, Silva RG, Mendes MA, Basso LA, Palma MS, de Azevedo WF, Santos DS, Biochem Biophys Res Commun. 2004 Jan 23;313(4):907-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14706628 14706628]
Structures of human purine nucleoside phosphorylase complexed with inosine and ddI., Canduri F, dos Santos DM, Silva RG, Mendes MA, Basso LA, Palma MS, de Azevedo WF, Santos DS, Biochem Biophys Res Commun. 2004 Jan 23;313(4):907-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14706628 14706628]
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Application of crystallographic and modeling methods in the design of purine nucleoside phosphorylase inhibitors., Ealick SE, Babu YS, Bugg CE, Erion MD, Guida WC, Montgomery JA, Secrist JA 3rd, Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11540-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1763067 1763067]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Purine-nucleoside phosphorylase]]
[[Category: Purine-nucleoside phosphorylase]]
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[[Category: Purine nucleoside phosphorylase]]
[[Category: Purine nucleoside phosphorylase]]
[[Category: Synchrotron]]
[[Category: Synchrotron]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:18:46 2008''

Revision as of 23:18, 27 July 2008

Image:1rct.png

Template:STRUCTURE 1rct

Crystal structure of Human purine nucleoside phosphorylase complexed with INOSINE

Template:ABSTRACT PUBMED 14706628

About this Structure

1RCT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structures of human purine nucleoside phosphorylase complexed with inosine and ddI., Canduri F, dos Santos DM, Silva RG, Mendes MA, Basso LA, Palma MS, de Azevedo WF, Santos DS, Biochem Biophys Res Commun. 2004 Jan 23;313(4):907-14. PMID:14706628

Application of crystallographic and modeling methods in the design of purine nucleoside phosphorylase inhibitors., Ealick SE, Babu YS, Bugg CE, Erion MD, Guida WC, Montgomery JA, Secrist JA 3rd, Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11540-4. PMID:1763067

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