1pfl
From Proteopedia
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REFINED SOLUTION STRUCTURE OF HUMAN PROFILIN I
Overview
Profilin is a ubiquitous eukaryotic protein that binds to both cytosolic, actin and the phospholipid phosphatidylinositol-4,5-bisphosphate. These, dual competitive binding capabilities of profilin suggest that profilin, serves as a link between the phosphatidyl inositol cycle and actin, polymerization, and thus profilin may be an essential component in the, signaling pathway leading to cytoskeletal rearrangement. The refined, three-dimensional solution structure of human profilin I has been, determined using multidimensional heteronuclear NMR spectroscopy. Twenty, structures were selected to represent the solution conformational, ensemble. This ensemble of structures has root-mean-square distance, deviations from the mean structure of 0.58 A for the backbone atoms and, 0.98 A for all non-hydrogen atoms. Comparison of the solution structure of, human profilin to the crystal structure of bovine profilin reveals that, although profilin adopts essentially identical conformations in both, states, the solution structure is more compact than the crystal structure., Interestingly, the regions that show the most structural diversity are, located at or near the actin-binding site of profilin. We suggest that, structural differences are reflective of dynamical properties of profilin, that facilitate favorable interactions with actin. The global folding, pattern of human profilin also closely resembles that of Acanthamoeba, profilin I, reflective of the 22% sequence identity and approximately 45%, sequence similarity between these two proteins.
About this Structure
1PFL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Refined solution structure of human profilin I., Metzler WJ, Farmer BT 2nd, Constantine KL, Friedrichs MS, Lavoie T, Mueller L, Protein Sci. 1995 Mar;4(3):450-9. PMID:7795529
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