Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We have determined a medium resolution three-dimensional solution structure of Acanthamoeba profilin-I by multidimensional nuclear magnetic resonance spectroscopy. This 13-kD actin binding protein consists of a five stranded antiparallel beta sheet flanked by NH2- and COOH-terminal helices on one face and by a third helix and a two stranded beta sheet on the other face. Data from actin-profilin cross-linking experiments and the localization of conserved residues between profilins in different phyla indicate that actin binding occurs on the molecular face occupied by the terminal helices. The other face of the molecule contains the residues that differ between Acanthamoeba profilins-I and II and may be important in determining the difference in polyphosphoinositide binding between these isoforms. This suggests that lipids and actin bind to different faces of the molecule.
Three-dimensional solution structure of Acanthamoeba profilin-I.,Vinson VK, Archer SJ, Lattman EE, Pollard TD, Torchia DA J Cell Biol. 1993 Sep;122(6):1277-83. PMID:8397216[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vinson VK, Archer SJ, Lattman EE, Pollard TD, Torchia DA. Three-dimensional solution structure of Acanthamoeba profilin-I. J Cell Biol. 1993 Sep;122(6):1277-83. PMID:8397216
