2fv2
From Proteopedia
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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.]] | ||
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Revision as of 01:20, 4 May 2008
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 >> 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 Structure
2FV2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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