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1x65

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Revision as of 13:05, 25 December 2014

Solution structure of the third cold-shock domain of the human KIAA0885 protein (UNR PROTEIN)

Structural highlights

1x65 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	UNR (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum, TOPSAN

Function

[CSDE1_HUMAN] RNA-binding protein. Required for internal initiation of translation of human rhinovirus RNA. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Upon cold shock, the amounts of most proteins dramatically decrease from normal levels, but those of cold shock proteins (CSPs) and proteins containing cold-shock domains (CSDs) greatly increase. Although their biological function is still not completely clear, cold-shock proteins might control translation via RNA chaperoning. Many cold-shock proteins contain the motifs (Y/F)GFI and (V/F)(V/F)H, which are known as ribonucleoprotein (RNP)-1 and RNP-2 motifs implicated in RNA/DNA binding. We determined the solution NMR structures of all five constituent CSDs of the human UNR (upstream of N-ras) protein. The spatial arrangements of the sidechains in the RNP-1 and RNP-2 motifs are mostly conserved; however, the conformations of the following residues in the first CSD are different: F43 and H45 (the first phenylalanine residue and the histidine residue in the putative binding site RNP-2) and Y30 (the first residue in the putative binding site RNP-1). F43 and H45 affect each other, and H45 is further influenced by C46. The altered binding site of the first CSD, and its putatively enhanced intrinsic stability, may provide an explanation for the observation that the first CSD has 20-fold higher RNA-binding activity than the fifth CSD. It also lends support to the hypothesis that the UNR protein arose by repeated duplication of a protein that originally contained just one CSD, and that the proto-UNR protein acquired cysteine C46 by mutation during evolution.

The NMR solution structures of the five constituent cold-shock domains (CSD) of the human UNR (upstream of N-ras) protein.,Goroncy AK, Koshiba S, Tochio N, Tomizawa T, Inoue M, Watanabe S, Harada T, Tanaka A, Ohara O, Kigawa T, Yokoyama S J Struct Funct Genomics. 2010 Jun;11(2):181-8. Epub 2010 Mar 6. PMID:20213426^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Grosset C, Chen CY, Xu N, Sonenberg N, Jacquemin-Sablon H, Shyu AB. A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex. Cell. 2000 Sep 29;103(1):29-40. PMID:11051545
↑ Chang TC, Yamashita A, Chen CY, Yamashita Y, Zhu W, Durdan S, Kahvejian A, Sonenberg N, Shyu AB. UNR, a new partner of poly(A)-binding protein, plays a key role in translationally coupled mRNA turnover mediated by the c-fos major coding-region determinant. Genes Dev. 2004 Aug 15;18(16):2010-23. PMID:15314026 doi:http://dx.doi.org/10.1101/gad.1219104
↑ Goroncy AK, Koshiba S, Tochio N, Tomizawa T, Inoue M, Watanabe S, Harada T, Tanaka A, Ohara O, Kigawa T, Yokoyama S. The NMR solution structures of the five constituent cold-shock domains (CSD) of the human UNR (upstream of N-ras) protein. J Struct Funct Genomics. 2010 Jun;11(2):181-8. Epub 2010 Mar 6. PMID:20213426 doi:10.1007/s10969-010-9081-z

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1x65"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1x65]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X65 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X65 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UNR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UNR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x65 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1x65 RCSB], [http://www.ebi.ac.uk/pdbsum/1x65 PDBsum], [http://www.topsan.org/Proteins/RSGI/1x65 TOPSAN]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x65 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1x65 RCSB], [http://www.ebi.ac.uk/pdbsum/1x65 PDBsum], [http://www.topsan.org/Proteins/RSGI/1x65 TOPSAN]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CSDE1_HUMAN CSDE1_HUMAN]] RNA-binding protein. Required for internal initiation of translation of human rhinovirus RNA. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain.<ref>PMID:11051545</ref> <ref>PMID:15314026</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 31: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Goroncy, A K.]]
+[[Category: Goroncy, A K]]
-[[Category: Inoue, M.]]
+[[Category: Inoue, M]]
-[[Category: Kigawa, T.]]
+[[Category: Kigawa, T]]
-[[Category: Kobayashi, N.]]
+[[Category: Kobayashi, N]]
-[[Category: Koshiba, S.]]
+[[Category: Koshiba, S]]
-[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
+[[Category: Structural genomic]]
-[[Category: Tochio, N.]]
+[[Category: Tochio, N]]
-[[Category: Yokoyama, S.]]
+[[Category: Yokoyama, S]]
 [[Category: Beta-barrel]]
 [[Category: Cell-free protein synthesis]]
@@ Line 43: / Line 45: @@
 [[Category: Nppsfa]]
 [[Category: Qb fold]]
-[[Category: Riken structural genomics/proteomics initiative]]
 [[Category: Rna binding protein]]
 [[Category: Rna chaperone]]
 [[Category: Rna/dna binding]]
 [[Category: Rsgi]]
-[[Category: Structural genomic]]
 [[Category: Translational regulation]]
 [[Category: Unr protein]]

1x65

From Proteopedia

Revision as of 13:05, 25 December 2014

Solution structure of the third cold-shock domain of the human KIAA0885 protein (UNR PROTEIN)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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