4dkk: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4dkk|  PDB=4dkk  |  SCENE=  }}
===The X-ray Crystal Structure of the Human STAU1 SSM-'RBD'5 Domain-Swapped Dimer===
{{ABSTRACT_PUBMED_23524536}}


The entry 4dkk is ON HOLD  until Mar 20 2014
==Function==
[[http://www.uniprot.org/uniprot/STAU1_HUMAN STAU1_HUMAN]] Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.


Authors: Gleghorn, M.L.
==About this Structure==
[[4dkk]] is a 1 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=4DKK OCA].  


Description: The X-ray Crystal Structure of the Human STAU1 SSM-'RBD'5 Domain-Swapped Dimer
==Reference==
<ref group="xtra">PMID:023524536</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Gleghorn, M L.]]
[[Category: Beta sheet]]
[[Category: Dimerization]]
[[Category: Protein binding]]
[[Category: Rbd]]
[[Category: Rna binding protein]]
[[Category: Swapping-motif]]

Revision as of 15:05, 19 June 2013

Template:STRUCTURE 4dkk

The X-ray Crystal Structure of the Human STAU1 SSM-'RBD'5 Domain-Swapped Dimer

Template:ABSTRACT PUBMED 23524536

Function

[STAU1_HUMAN] Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.

About this Structure

4dkk is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  1. Gleghorn ML, Gong C, Kielkopf CL, Maquat LE. Staufen1 dimerizes through a conserved motif and a degenerate dsRNA-binding domain to promote mRNA decay. Nat Struct Mol Biol. 2013 Apr;20(4):515-24. doi: 10.1038/nsmb.2528. Epub 2013 Mar, 24. PMID:23524536 doi:10.1038/nsmb.2528

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