1ndl: Difference between revisions

Revision as of 07:38, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ndl.png

Template:STRUCTURE 1ndl

THE AWD NUCLEOTIDE DIPHOSPHATE KINASE FROM DROSOPHILATHE AWD NUCLEOTIDE DIPHOSPHATE KINASE FROM DROSOPHILA

Template:ABSTRACT PUBMED 8081741

About this StructureAbout this Structure

1NDL is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the Awd nucleotide diphosphate kinase from Drosophila., Chiadmi M, Morera S, Lascu I, Dumas C, Le Bras G, Veron M, Janin J, Structure. 1993 Dec 15;1(4):283-93. PMID:8081741

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-'''THE AWD NUCLEOTIDE DIPHOSPHATE KINASE FROM DROSOPHILA'''
+===THE AWD NUCLEOTIDE DIPHOSPHATE KINASE FROM DROSOPHILA===
-==Overview==
+<!--
-BACKGROUND: Nucleotide diphosphate kinase (NDP kinase) is a phosphate transfer enzyme involved in cell regulation and in animal development. Drosophila NDP kinase is the product of the abnormal wing disc (awd) developmental gene, a point mutation in which can produce the killer of prune (K-pn) conditional lethal phenotype. The highly homologous mammalian genes control metastasis and a human NDP kinase acts as a transcription factor. RESULTS: The X-ray structure of the Awd protein prepared from Drosophila was solved at 2.4 A resolution by molecular replacement from the homologous Dictyostelium protein. Both are hexamers, and both have the same fold and the same active site. Subunit contacts differ as a result of sequence changes in the carboxy-terminal segment and in the loop that is the site of the K-pn mutation. CONCLUSIONS: Regulatory properties of animal NDP kinases depend on interactions with other macromolecules, such as DNA and the product of the Drosophila prune gene. The Awd structure suggests an allosteric mechanism of action of NDP kinase where DNA is the effector and the protein undergoes a major conformational change, possibly dissociating to dimers.
+The line below this paragraph, {{ABSTRACT_PUBMED_8081741}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8081741 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_8081741}}
 ==About this Structure==
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 [[Category: Veron, M.]]
 [[Category: Phosphotransferase]]
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