1g9l
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g9l OCA], [http://www.ebi.ac.uk/pdbsum/1g9l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g9l RCSB]</span> | ||
}} | }} | ||
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[[Category: all-helical domain]] | [[Category: all-helical domain]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:39:39 2008'' |
Revision as of 17:39, 30 March 2008
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
SOLUTION STRUCTURE OF THE PABC DOMAIN OF HUMAN POLY(A) BINDING PROTEIN
Overview
We have determined the solution structure of the C-terminal quarter of human poly(A)-binding protein (hPABP). The protein fragment contains a protein domain, PABC [for poly(A)-binding protein C-terminal domain], which is also found associated with the HECT family of ubiquitin ligases. By using peptides derived from PABP interacting protein (Paip) 1, Paip2, and eRF3, we show that PABC functions as a peptide binding domain. We use chemical shift perturbation analysis to identify the peptide binding site in PABC and the major elements involved in peptide recognition. From comparative sequence analysis of PABC-binding peptides, we formulate a preliminary PABC consensus sequence and identify human ataxin-2, the protein responsible for type 2 spinocerebellar ataxia (SCA2), as a potential PABC ligand.
About this Structure
1G9L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure and function of the C-terminal PABC domain of human poly(A)-binding protein., Kozlov G, Trempe JF, Khaleghpour K, Kahvejian A, Ekiel I, Gehring K, Proc Natl Acad Sci U S A. 2001 Apr 10;98(8):4409-13. Epub 2001 Apr 3. PMID:11287632
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