Document Detail


Ser/Thr motifs in transmembrane proteins: conservation patterns and effects on local protein structure and dynamics.
MedLine Citation:
PMID:  22836667     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We combined systematic bioinformatics analyses and molecular dynamics simulations to assess the conservation patterns of Ser and Thr motifs in membrane proteins, and the effect of such motifs on the structure and dynamics of α-helical transmembrane (TM) segments. We find that Ser/Thr motifs are often present in β-barrel TM proteins. At least one Ser/Thr motif is present in almost half of the sequences of α-helical proteins analyzed here. The extensive bioinformatics analyses and inspection of protein structures led to the identification of molecular transporters with noticeable numbers of Ser/Thr motifs within the TM region. Given the energetic penalty for burying multiple Ser/Thr groups in the membrane hydrophobic core, the observation of transporters with multiple membrane-embedded Ser/Thr is intriguing and raises the question of how the presence of multiple Ser/Thr affects protein local structure and dynamics. Molecular dynamics simulations of four different Ser-containing model TM peptides indicate that backbone hydrogen bonding of membrane-buried Ser/Thr hydroxyl groups can significantly change the local structure and dynamics of the helix. Ser groups located close to the membrane interface can hydrogen bond to solvent water instead of protein backbone, leading to an enhanced local solvation of the peptide.
Authors:
Coral Del Val; Stephen H White; Ana-Nicoleta Bondar
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-07-27
Journal Detail:
Title:  The Journal of membrane biology     Volume:  245     ISSN:  1432-1424     ISO Abbreviation:  J. Membr. Biol.     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-10-29     Completed Date:  2013-05-07     Revised Date:  2014-02-05    
Medline Journal Info:
Nlm Unique ID:  0211301     Medline TA:  J Membr Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  717-30     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Motifs
Amino Acid Sequence
Computational Biology
Conserved Sequence
Hydrogen Bonding
Membrane Proteins / chemistry*
Membrane Transport Proteins / chemistry
Molecular Dynamics Simulation
Peptides / chemistry
Protein Conformation
Receptors, Cell Surface / chemistry
Serine / chemistry*
Threonine / chemistry*
Grant Support
ID/Acronym/Agency:
GM-74637/GM/NIGMS NIH HHS; R01 GM074637/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Membrane Proteins; 0/Membrane Transport Proteins; 0/Peptides; 0/Receptors, Cell Surface; 2ZD004190S/Threonine; 452VLY9402/Serine
Comments/Corrections

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


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