Refined solution structure of human profilin I data
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Three-dimensional solution structure of Acanthamoeba profilin-I
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...
متن کاملIdentification of the poly-L-proline-binding site on human profilin.
Profilin is a ubiquitous protein that has been implicated in the signaling pathway leading to cytoskeletal rearrangement in cells. An unusual property of profilin is its high binding affinity for poly-L-proline (PLP). This binding property is conserved in the profilins from diverse species with little sequence homology. We have monitored the binding of PLP to profilin by fluorescence and nuclea...
متن کاملساختار بلوری کمپلکس(٢،'٢- بی پیریدین) (۲ ،۵ – دی کلروفنیل سیانامیدو) (۲ ،'٢:'۶،"۲-ترپیریدین) رودیم(III) هگزافلوئوروفسفات [Rh(terpy)(bpy)(2,5-Cl2pcyd)](PF6)2.0.5CH3CN
The first crystal structure of a phenylcyanamide Rh(III) complex, [Rh(terpy)(bpy)(2,5-Cl2pcyd)](PF6)2 (terpy = 2,2΄:6′,2″– terpyridine, bpy= 2,2΄-bipyridine, and 2,5-Cl2pcyd = 2,5-dichlorophenylcyanamide) has been reported in this paper. Crystals of [Rh(terpy)(bpy)(2,5-Cl2pcyd)](PF6)2 .0.5CH3CN were grown by ether diffusion into an acetonitrile solution of the complex. Crystal structure data: o...
متن کاملIncompatibility with formin Cdc12p prevents human profilin from substituting for fission yeast profilin: insights from crystal structures of fission yeast profilin.
Expression of human profilin-I does not complement the temperature-sensitive cdc3-124 mutation of the single profilin gene in fission yeast Schizosaccharomyces pombe, resulting in death from cytokinesis defects. Human profilin-I and S. pombe profilin have similar affinities for actin monomers, the FH1 domain of fission yeast formin Cdc12p and poly-L-proline (Lu, J., and Pollard, T. D. (2001) Mo...
متن کاملElucidation of the poly-L-proline binding site in Acanthamoeba profilin I by NMR spectroscopy.
The multifunctional protein profilin is one of the most abundant proteins in the cytoplasm and is thought to regulate actin assembly and the phosphoinositide signaling pathway. Profilin binds to several different ligands including actin, poly-L-proline, and the head groups of polyphosphoinositides. Knowledge of profilin/ligand interactions is important for understanding the physiology of profil...
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تاریخ انتشار 1994