1cz9: Difference between revisions

Revision as of 21:51, 30 June 2008

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File:1cz9.png

Template:STRUCTURE 1cz9

ATOMIC RESOLUTION ASV INTEGRASE CORE DOMAIN (D64N) FROM CITRATEATOMIC RESOLUTION ASV INTEGRASE CORE DOMAIN (D64N) FROM CITRATE

Template:ABSTRACT PUBMED 10521258

About this StructureAbout this Structure

1CZ9 is a Single protein structure of sequence from Avian sarcoma virus. Full crystallographic information is available from OCA.

ReferenceReference

Atomic resolution structures of the core domain of avian sarcoma virus integrase and its D64N mutant., Lubkowski J, Dauter Z, Yang F, Alexandratos J, Merkel G, Skalka AM, Wlodawer A, Biochemistry. 1999 Oct 12;38(41):13512-22. PMID:10521258

Page seeded by OCA on Mon Jun 30 21:51:04 2008

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OCA

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-'''ATOMIC RESOLUTION ASV INTEGRASE CORE DOMAIN (D64N) FROM CITRATE'''
+===ATOMIC RESOLUTION ASV INTEGRASE CORE DOMAIN (D64N) FROM CITRATE===
-==Overview==
+<!--
-Six crystal structures of the core domain of integrase (IN) from avian sarcoma virus (ASV) and its active-site derivative containing an Asp64 --&gt; Asn substitution have been solved at atomic resolution ranging 1.02-1.42 A. The high-quality data provide new structural information about the active site of the enzyme and clarify previous inconsistencies in the description of this fragment. The very high resolution of the data and excellent quality of the refined models explain the dynamic properties of IN and the multiple conformations of its disordered residues. They also allow an accurate description of the solvent structure and help to locate other molecules bound to the enzyme. A detailed analysis of the flexible active-site region, in particular the loop formed by residues 144-154, suggests conformational changes which may be associated with substrate binding and enzymatic activity. The pH-dependent conformational changes of the active-site loop correlates with the pH vs activity profile observed for ASV IN.
+The line below this paragraph, {{ABSTRACT_PUBMED_10521258}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_10521258}}
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