2fv2
From Proteopedia
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|PDB= 2fv2 |SIZE=350|CAPTION= <scene name='initialview01'>2fv2</scene>, resolution 2.20Å | |PDB= 2fv2 |SIZE=350|CAPTION= <scene name='initialview01'>2fv2</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Rcd1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= Rcd1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Gillon, W.]] | [[Category: Gillon, W.]] | ||
[[Category: Pai, E F.]] | [[Category: Pai, E F.]] | ||
| - | [[Category: MN]] | ||
[[Category: armadillo-repeat]] | [[Category: armadillo-repeat]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:08:02 2008'' |
Revision as of 00:08, 31 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | Rcd1 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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