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| - | [[Image:2fv2.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2fv2| PDB=2fv2 | SCENE= }} | | {{STRUCTURE_2fv2| PDB=2fv2 | SCENE= }} |
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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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| - | ==Overview==
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| - | 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.
| + | 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. |
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| | + | {{ABSTRACT_PUBMED_17189474}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pai, E F.]] | | [[Category: Pai, E F.]] |
| | [[Category: Armadillo-repeat]] | | [[Category: Armadillo-repeat]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:20:27 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:53:27 2008'' |
Revision as of 10:53, 28 July 2008
Template:STRUCTURE 2fv2
Crystal Structure Analysis of human Rcd-1 conserved region
Template:ABSTRACT PUBMED 17189474
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
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