Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

Mutations affecting the oligomerization interface of G-protein-coupled receptors revealed by a novel de novo protein design framework.

Mutations affecting the oligomerization interface of G-protein-coupled receptors revealed by a novel de novo protein design framework. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

  • Abstract Text of This Paper
  • Journal Published
  • MeSH Keywords of This Abstract
  • Chemicals and Substances Used in this Paper
  • Grants and Granting Agency of this Research
  • Database Accession Numbers Used in this Paper
  • Related Papers
  • Related Research Tags
  • Rate this Research Paper
  • Mutations affecting the oligomerization interface of G-protein-coupled receptors revealed by a novel de novo protein design framework. Abstract Text:

    martin s taylorMartin S Taylor,ho k fungHo K Fung,rohit rajgariaRohit Rajgaria,marta filizolaMarta Filizola,harel weinsteinHarel Weinstein,christodoulos a floudasChristodoulos A Floudas,

    Specific functional and pharmacological properties have recently been ascribed to G-protein-coupled receptor (GPCR) dimers/oligomers. Because the association of two identical or two distinct GPCR monomers seems to be required to elicit receptor function, it is necessary to understand the exact nature of this interaction. We present here a novel method for de novo protein design and its application to the prediction of mutations that can stabilize or destabilize a GPCR dimer while maintaining the monomer's native fold. To test the efficacy of this new method, the dimer of the single-spanned transmembrane domain of glycophorin A was used as a model system. Experimental data from mutagenesis of the helix-helix interface are compared with computational predictions at that interface, and the model's results are found to be consistent with the experimental findings. A flexible template was developed for the rhodopsin homodimer at atomic resolution and used to predict sets of three and five mutations. The results are found to be consistent across eight case studies, with favored mutations at each position. Mutation sets predicted to be the most disruptive at the dimerization interface are found to be less specific to the flexible template than sets predicted to be less disruptive.

    Mutations affecting the oligomerization interface of G-protein-coupled receptors revealed by a novel de novo protein design framework. Publishing Authors By Initials

    ms taylorMS Taylor,hk fungHK Fung,r rajgariaR Rajgaria,m filizolaM Filizola,h weinsteinH Weinstein,ca floudasCA Floudas,

    For similar abstracts research abstracts see: abstracts research

    PUBMED ID PMID:

    MEDLINE DATE:

    Mutations affecting the oligomerization interface of G-protein-coupled receptors revealed by a novel de novo protein design framework. Journal Published:

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: Biophysical journal

    VOLUME: 94

    Page Numbers: 2470-81

    Journal Abbreviation: Biophys. J.

    ISSN: 1542-0086

    DAY: 4

    MONTH: 01

    YEAR: 2008

    Mutations affecting the oligomerization interface of G-protein-coupled receptors revealed by a novel de novo protein design framework. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 370626

    Mutations affecting the oligomerization interface of G-protein-coupled receptors revealed by a novel de novo protein design framework. Keywords Mesh Terms:

    KEYWORDS:

    MESH TERMS:

    Chemical & Substance for Abstract: Mutations affecting the oligomerization interface of G-protein-coupled receptors revealed by a novel de novo protein design framework. Information

    Substance Name:

    Registry Number:

    Grant and Affiliation Information for Mutations affecting the oligomerization interface of G-protein-coupled receptors revealed by a novel de novo protein design framework.

    AFFILIATION: Department of Chemical Engineering, Princeton University, Princeton, New Jersey 08544, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIGMS

    GRANT: R24 GM069736

    ACRONYM: GM

    MEDLINETA: Biophys J

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Mutations affecting the oligomerization interface of G-protein-coupled receptors revealed by a novel de novo protein design framework Related Publications

     

    Molecular Station USER Menu

    Welcome to Molecular Station!

    You have to register before you can post on our forums or use our advanced features. Register Now! Its Free and Fast!

    Already registered? Login now below.

    User Name:

    Password:

    Already registered and Forgot your password? Click below to recover it.

    Recover Lost Password

    Join now - it's fast and free!

    Molecular Station is THE largest network of researchers, scientists and science lovers anywhere!

    Research Terms of Usage and Disclaimer
    Home
    Features

    Protocols

    DNA Forum

    Science Forum

    DNA Forum
    Biology Forum

    Science News


    [CaRP] XML error: Invalid document end at line 2

    For more click here:Science News