1nue: Difference between revisions

Revision as of 10:08, 28 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:1nue.png

Template:STRUCTURE 1nue

X-RAY STRUCTURE OF NM23 HUMAN NUCLEOSIDE DIPHOSPHATE KINASE B COMPLEXED WITH GDP AT 2 ANGSTROMS RESOLUTIONX-RAY STRUCTURE OF NM23 HUMAN NUCLEOSIDE DIPHOSPHATE KINASE B COMPLEXED WITH GDP AT 2 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 8747457

About this StructureAbout this Structure

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

ReferenceReference

X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution., Morera S, Lacombe ML, Xu Y, LeBras G, Janin J, Structure. 1995 Dec 15;3(12):1307-14. PMID:8747457

Page seeded by OCA on Mon Jul 28 10:08:18 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1nue.gif|left|200px]]
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-'''X-RAY STRUCTURE OF NM23 HUMAN NUCLEOSIDE DIPHOSPHATE KINASE B COMPLEXED WITH GDP AT 2 ANGSTROMS RESOLUTION'''
+===X-RAY STRUCTURE OF NM23 HUMAN NUCLEOSIDE DIPHOSPHATE KINASE B COMPLEXED WITH GDP AT 2 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-BACKGROUND: Nucleoside diphosphate (NDP) kinases provide precursors for DNA and RNA synthesis. In mammals, these enzymes are also involved in cell regulations. Human NDP kinase B, product of the human nm23-H2 gene, is both an enzyme and a transcription factor. It activates transcription of the c-myc oncogene independently of its catalytic function, by binding to its promoter DNA. How do the two functions coexist? RESULTS: Recombinant human NDP kinase B was co-crystallized with GDP. The X-ray structure was solved at 2.0 A resolution by molecular replacement from the homologous Drosophila Awd protein. Both enzymes are homo-hexamers with a characteristic beta alpha beta beta alpha beta fold. GDP binds near the active site His118. The guanine base is in a surface cleft and interacts with the C terminus of another subunit. CONCLUSIONS: The beta alpha beta beta alpha beta fold, also present in the 'palm' domain of Escherichia coli DNA polymerase I and HIV reverse transcriptase, is both a mononucleotide- and a polynucleotide-binding fold. If NDP kinase B binds DNA in the same way as the polymerases, the enzyme must undergo a conformation change in order to carry out gene activation.
+The line below this paragraph, {{ABSTRACT_PUBMED_8747457}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8747457 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8747457}}
 ==About this Structure==
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 [[Category: Nucleoside diphosphate]]
 [[Category: Nucleoside triphosphate]]
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