3kur
From Proteopedia
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===Crystal structure of the MLLE domain of poly(A)-binding protein=== | ===Crystal structure of the MLLE domain of poly(A)-binding protein=== | ||
+ | {{ABSTRACT_PUBMED_20096703}} | ||
- | + | ==Function== | |
- | + | [[http://www.uniprot.org/uniprot/PABP1_HUMAN PABP1_HUMAN]] Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. 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. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed.<ref>PMID:11051545</ref> <ref>PMID:18447585</ref> | |
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==About this Structure== | ==About this Structure== | ||
- | + | [[3kur]] is a 8 chain structure with 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=3KUR OCA]. | |
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020096703</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Gehring, K.]] | [[Category: Gehring, K.]] | ||
[[Category: Kozlov, G.]] | [[Category: Kozlov, G.]] | ||
- | [[Category: Acetylation]] | ||
[[Category: All-helical domain]] | [[Category: All-helical domain]] | ||
- | [[Category: Alternative splicing]] | ||
- | [[Category: Cytoplasm]] | ||
[[Category: Methylation]] | [[Category: Methylation]] | ||
[[Category: Mrna processing]] | [[Category: Mrna processing]] | ||
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[[Category: Rna-binding]] | [[Category: Rna-binding]] | ||
[[Category: Spliceosome]] | [[Category: Spliceosome]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 24 08:22:07 2010'' |
Revision as of 19:57, 4 April 2013
Contents |
Crystal structure of the MLLE domain of poly(A)-binding protein
Template:ABSTRACT PUBMED 20096703
Function
[PABP1_HUMAN] Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. 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. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed.[1] [2]
About this Structure
3kur is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Kozlov G, Menade M, Rosenauer A, Nguyen L, Gehring K. Molecular determinants of PAM2 recognition by the MLLE domain of poly(A)-binding protein. J Mol Biol. 2010 Mar 26;397(2):397-407. Epub 2010 Jan 22. PMID:20096703 doi:10.1016/j.jmb.2010.01.032
- ↑ 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
- ↑ Singh G, Rebbapragada I, Lykke-Andersen J. A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay. PLoS Biol. 2008 Apr 29;6(4):e111. doi: 10.1371/journal.pbio.0060111. PMID:18447585 doi:10.1371/journal.pbio.0060111