2l42

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[[Image:2l42.png|left|200px]]
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==The solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae==
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<StructureSection load='2l42' size='340' side='right' caption='[[2l42]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2l42]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L42 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L42 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAP1, GRF1, TUF1, YNL216W, N1310 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l42 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l42 RCSB], [http://www.ebi.ac.uk/pdbsum/2l42 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Rap1 (repressor-activator protein 1) from Saccharomyces cerevisiae, containing a BRCT domain at its N-terminus, is a multifunctional protein that controls telomere function, silencing, and the activation of glycolytic and ribosomal protein genes. In this work, we determined the solution structure of Rap1 BRCT domain, which contains three beta-strands and three alpha-helices. Structural comparison indicated that Rap1 BRCT domain adopts a global fold similar to other BRCT domains, implying some common structural aspects of BRCT domain family. On the other hand, Rap1 BRCT domain displays structural characteristics significantly different from other BRCT domains in that Rap1 BRCT domain adopts a rather flexible conformation with less secondary structure elements, revealing a novel fold of the BRCT domain family.
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{{STRUCTURE_2l42| PDB=2l42 | SCENE= }}
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Solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae reveals a novel fold.,Zhang W, Zhang J, Zhang X, Xu C, Tu X Biochem Biophys Res Commun. 2010 Dec 25. PMID:21187076<ref>PMID:21187076</ref>
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===The solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_21187076}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2l42]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L42 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:021187076</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Tu, X.]]
[[Category: Tu, X.]]

Revision as of 11:32, 20 October 2014

The solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae

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