1b64: Difference between revisions

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New page: left|200px<br /> <applet load="1b64" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b64" /> '''SOLUTION STRUCTURE OF THE GUANINE NUCLEOTID...
 
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==About this Structure==
==About this Structure==
1B64 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B64 OCA]].  
1B64 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Structure known Active Site: GEF. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B64 OCA]].  


==Reference==
==Reference==
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[[Category: translation elongation]]
[[Category: translation elongation]]


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Revision as of 09:25, 30 October 2007

File:1b64.gif


1b64

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SOLUTION STRUCTURE OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR DOMAIN FROM HUMAN ELONGATION FACTOR-ONE BETA, NMR, 20 STRUCTURES

OverviewOverview

BACKGROUND: In eukaryotic protein synthesis, the multi-subunit elongation, factor 1 (EF-1) plays an important role in ensuring the fidelity and, regulating the rate of translation. EF-1alpha, which transports the, aminoacyl tRNA to the ribosome, is a member of the G-protein superfamily., EF-1beta regulates the activity of EF-1alpha by catalyzing the exchange of, GDP for GTP and thereby regenerating the active form of EF-1alpha. The, structure of the bacterial analog of EF-1alpha, EF-Tu has been solved in, complex with its GDP exchange factor, EF-Ts. These structures indicate a, mechanism for GDP-GTP exchange in prokaryotes. Although there is good, sequence conservation between EF-1alpha and EF-Tu, there is essentially no, sequence similarity between EF-1beta and EF-Ts. We wished to ... [(full description)]

About this StructureAbout this Structure

1B64 is a [Single protein] structure of sequence from [Homo sapiens]. Structure known Active Site: GEF. Full crystallographic information is available from [OCA].

ReferenceReference

The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli., Perez JM, Siegal G, Kriek J, Hard K, Dijk J, Canters GW, Moller W, Structure. 1999 Feb 15;7(2):217-26. PMID:10368288

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