2fv2
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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 with as ligand. 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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