Document Detail


Structures of the pleckstrin homology domain of Saccharomyces cerevisiae Avo1 and its human orthologue Sin1, an essential subunit of TOR complex 2.
MedLine Citation:
PMID:  22505404     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In eukaryotes, multiprotein complexes termed TOR complex 1 (TORC1) and TOR complex 2 (TORC2) function as major regulators of cell growth, metabolism and ageing. The C-terminal domain of the Saccharomyces cerevisiae TORC2 component Avo1 is required for plasma-membrane localization of TORC2 and is essential for yeast viability. X-ray crystal structures of the C-terminal domain of Avo1 and of its human orthologue Sin1 have been determined. The structures show that the C-termini of Avo1 and Sin1 both have the pleckstrin homology (PH) domain fold. Comparison with known PH-domain structures suggests a putative binding site for phosphoinositides.
Authors:
Dongqing Pan; Yoshiyuki Matsuura
Related Documents :
24663024 - Preclinical profile of bi 224436, a novel hiv-1 non-catalytic site integrase inhibitor.
23988114 - Interactions between hiv-1 vif and human elonginb-elonginc are important for cbf-beta b...
24004664 - Ubiquitination site preferences in anaphase promoting complex/cyclosome (apc/c) substra...
23566874 - Functional characterization of a novel tropinone reductase-like gene in dendrobium nobi...
2693124 - Hiv-1 protease: mutagenesis of asparagine 88 indicates a domain required for dimer form...
24663024 - Preclinical profile of bi 224436, a novel hiv-1 non-catalytic site integrase inhibitor.
Publication Detail:
Type:  Journal Article     Date:  2012-03-27
Journal Detail:
Title:  Acta crystallographica. Section F, Structural biology and crystallization communications     Volume:  68     ISSN:  1744-3091     ISO Abbreviation:  Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-04-16     Completed Date:  2012-06-25     Revised Date:  2014-04-01    
Medline Journal Info:
Nlm Unique ID:  101226117     Medline TA:  Acta Crystallogr Sect F Struct Biol Cryst Commun     Country:  England    
Other Details:
Languages:  eng     Pagination:  386-92     Citation Subset:  IM    
Copyright Information:
© 2012 International Union of Crystallography. All rights reserved.
Data Bank Information
Bank Name/Acc. No.:
PDB/3ULB;  3ULC;  3VOQ
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Adaptor Proteins, Signal Transducing / chemistry*
Amino Acid Sequence
Carrier Proteins / chemistry*
Humans
Models, Molecular
Molecular Sequence Data
Protein Structure, Quaternary
Protein Structure, Tertiary
Protein Subunits / chemistry
Saccharomyces cerevisiae / chemistry*
Saccharomyces cerevisiae Proteins / chemistry*
Sequence Alignment
Structural Homology, Protein
Transcription Factors / chemistry
Chemical
Reg. No./Substance:
0/Adaptor Proteins, Signal Transducing; 0/Avo1 protein, S cerevisiae; 0/CRTC2 protein, human; 0/Carrier Proteins; 0/MAPKAP1 protein, human; 0/Protein Subunits; 0/Saccharomyces cerevisiae Proteins; 0/Transcription Factors
Comments/Corrections

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


Previous Document:  Structure of MurA (UDP-N-acetylglucosamine enolpyruvyl transferase) from Vibrio fischeri in complex ...
Next Document:  Structure of the tetradecanucleotide d(CCCCGGTACCGGGG)2 as an A-DNA duplex.