2fv2: Difference between revisions

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[[Image:2fv2.gif|left|200px]]
[[Image:2fv2.gif|left|200px]]


{{Structure
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|GENE= Rcd1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_2fv2| PDB=2fv2 |  SCENE= }}  
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fv2 OCA], [http://www.ebi.ac.uk/pdbsum/2fv2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fv2 RCSB]</span>
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'''Crystal Structure Analysis of human Rcd-1 conserved region'''
'''Crystal Structure Analysis of human Rcd-1 conserved region'''
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[[Category: Gillon, W.]]
[[Category: Gillon, W.]]
[[Category: Pai, E F.]]
[[Category: Pai, E F.]]
[[Category: armadillo-repeat]]
[[Category: Armadillo-repeat]]
 
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Revision as of 04:20, 4 May 2008

File:2fv2.gif

Template:STRUCTURE 2fv2

Crystal Structure Analysis of human Rcd-1 conserved region


OverviewOverview

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 >> 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.

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 Page seeded by OCA on Sun May 4 04:20:27 2008

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