2fv2: Difference between revisions
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[[Image:2fv2.gif|left|200px]] | [[Image:2fv2.gif|left|200px]] | ||
'''Crystal Structure Analysis of human Rcd-1 conserved region''' | {{Structure | ||
|PDB= 2fv2 |SIZE=350|CAPTION= <scene name='initialview01'>2fv2</scene>, resolution 2.20Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | |||
|ACTIVITY= | |||
|GENE= Rcd1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Crystal Structure Analysis of human Rcd-1 conserved region''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2FV2 is a [ | 2FV2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FV2 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17189474 17189474] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: armadillo-repeat]] | [[Category: armadillo-repeat]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:57:07 2008'' |
Revision as of 17:57, 20 March 2008
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, resolution 2.20Å | |||||||
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Ligands: | |||||||
Gene: | Rcd1 (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
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