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: Actin-binding protein complexes at atomic resolution.
    Author: McLaughlin PJ, Weeds AG.
    Journal: Annu Rev Biophys Biomol Struct; 1995; 24():643-75. PubMed ID: 7663130.
    Abstract:
    This review describes three structures of actin complexed with different monomer-binding proteins, namely with DNase I, gelsolin segment 1, and profilin. In these proteins, the binding sites are discontinuous in the sequence, and those residues that form intermolecular hydrogen bonds are not well conserved in homologous proteins. The strongly conserved residues that define the family of proteins in gelsolin and profilin reflect the underlying structural fold of each. The binding surfaces for segment 1 and profilin are different, although they peripherally overlap on actin. No extreme features in the binding surfaces of these complexes distinguish them from other globular proteins.
    [Abstract] [Full Text] [Related] [New Search]