2fv2: Difference between revisions

Revision as of 13:53, 28 July 2008

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File:2fv2.png

Template:STRUCTURE 2fv2

Crystal Structure Analysis of human Rcd-1 conserved regionCrystal Structure Analysis of human Rcd-1 conserved region

Template:ABSTRACT PUBMED 17189474

About this StructureAbout this Structure

2FV2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Atomic model of human Rcd-1 reveals an armadillo-like-repeat protein with in vitro nucleic acid binding properties., Garces RG, Gillon W, Pai EF, Protein Sci. 2007 Feb;16(2):176-88. Epub 2006 Dec 22. PMID:17189474

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OCA

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-[[Image:2fv2.gif|left|200px]]
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 {{STRUCTURE_2fv2|  PDB=2fv2  |  SCENE=  }}
-'''Crystal Structure Analysis of human Rcd-1 conserved region'''
+===Crystal Structure Analysis of human Rcd-1 conserved region===
-==Overview==
+<!--
-Rcd-1, a protein highly conserved across eukaryotes, was initially identified as a factor essential for nitrogen starvation-invoked differentiation in fission yeast, and its Saccharomyces cerevisiae homolog, CAF40, has been identified as part of the CCR4-NOT transcription complex, where it interacts with the NOT1 protein. Mammalian homologs are involved in various cellular differentiation processes including retinoic acid-induced differentiation and hematopoetic cell development. Here, we present the 2.2 A X-ray structure of the highly conserved region of human Rcd-1 and investigate possible functional abilities of this and the full-length protein. The monomer is made up of six armadillo repeats forming a solvent-accessible, positively-charged cleft 21-22 A wide that, in contrast to other armadillo proteins, stays fully exposed in the dimer. Prompted by this finding, we established that Rcd-1 can bind to single- and double-stranded oligonucleotides in vitro with the affinity of G/C/T &gt;&gt; A. Mutation of an arginine residue within the cleft strongly reduced or abolished oligonucleotide binding. Rcd-1's ability to bind to nucleic acids, in addition to the previously reported protein-protein interaction with NOT1, suggests a new feature in Rcd-1's role in regulation of overall cellular differentiation processes.
+The line below this paragraph, {{ABSTRACT_PUBMED_17189474}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17189474 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17189474}}
 ==About this Structure==
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 [[Category: Pai, E F.]]
 [[Category: Armadillo-repeat]]
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