These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Correlation between binding and dynamics at SH2 domain interfaces.
    Author: Kay LE, Muhandiram DR, Wolf G, Shoelson SE, Forman-Kay JD.
    Journal: Nat Struct Biol; 1998 Feb; 5(2):156-63. PubMed ID: 9461082.
    Abstract:
    Protein recognition is a key determinant in regulating biological processes. Structures of complexes of interacting proteins provide significant insights into the mechanism of specific recognition. However, studies performed by modifying residues within a protein interface demonstrate that binding is not fully explained by these static pictures. Thus, structural data alone was not predictive of affinities in binding studies of phospholipase Cgamma1 and Syp phosphatase SH2 domains with phosphopeptides. NMR relaxation experiments probing dynamics of methyl groups of these complexes indicate a correlation between binding energy and restriction of motion at the interfacial region responsible for specific binding.
    [Abstract] [Full Text] [Related] [New Search]