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    A homology model of the Id-3 helix-loop-helix domain as a basis for structure-function predictions.

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    Authors
    Wibley, J
    Deed, Richard W
    Jasiok, M
    Douglas, K
    Norton, John D
    Affiliation
    Department of Pharmacy, University of Manchester, UK.
    Issue Date
    1996-05-23
    
    Metadata
    Show full item record
    Abstract
    The function of the dominant negative Id (inhibitor of differentiation) helix-loop-helix (HLH) proteins is to dimerize with, and prevent the DNA binding of basic HLH (bHLH) transcription factors. A three-dimensional homology model was constructed for the HLH domain of human Id3 based on the X-ray crystal structures of the E47, MyoD, and Max bHLH proteins. The model showed that, in contrast to bHLH proteins, Id proteins appear able to dimerize without DNA stabilization because of better packing of the hydrophobic core, and the absence of destabilizing polar loop residues and of repulsive positive charges in the monomer interface at the base of the four alpha-helix bundle. This prediction was tested by in vitro protein-binding experiments, which showed that Id3 did indeed self-associate. It also showed that the inability of Id proteins to bind DNA arises from the non-basic, poorly defined, random coil structure of the region corresponding to that responsible for bHLH DNA-binding. A model of the Id1 protein was constructed and revealed a potential site of charge-charge repulsion in the hypothetical homodimer interface that may explain its observed inability to form homodimers.
    Citation
    A homology model of the Id-3 helix-loop-helix domain as a basis for structure-function predictions. 1996, 1294 (2):138-46 Biochim. Biophys. Acta
    Journal
    Biochimica et Biophysica Acta
    URI
    http://hdl.handle.net/10541/95529
    DOI
    10.1016/0167-4838(96)00008-8
    PubMed ID
    8645731
    Type
    Article
    Language
    en
    ISSN
    0006-3002
    ae974a485f413a2113503eed53cd6c53
    10.1016/0167-4838(96)00008-8
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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