Structural aspects of actin-binding proteins

Curr Opin Cell Biol. 1994 Feb;6(1):87-95. doi: 10.1016/0955-0674(94)90121-x.

Abstract

The three-dimensional structures of myosin subfragment 1 (S1), gelsolin segment 1 complexed with alpha-actin, villin fragment 14T, Acanthamoeba profilin-I, and bovine profilin complexed with beta-actin were completed last year. Together, they expand our understanding of the structural organization of actin-binding proteins. In addition, the segment 1 and bovine profilin complexes provide atomic-level descriptions of their interfaces with actin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Actins / chemistry*
  • Actins / metabolism
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism
  • Gelsolin / chemistry
  • Gelsolin / metabolism
  • Humans
  • Microfilament Proteins / chemistry*
  • Microfilament Proteins / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Myosin Subfragments / chemistry
  • Myosin Subfragments / metabolism
  • Protein Structure, Secondary*

Substances

  • Actins
  • Carrier Proteins
  • Gelsolin
  • Microfilament Proteins
  • Myosin Subfragments
  • villin