1pfl

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[[Image:1pfl.gif|left|200px]]
[[Image:1pfl.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1pfl", creates the "Structure Box" on the page.
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|GENE= HUMAN PROFILIN CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1pfl| PDB=1pfl | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pfl OCA], [http://www.ebi.ac.uk/pdbsum/1pfl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pfl RCSB]</span>
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'''REFINED SOLUTION STRUCTURE OF HUMAN PROFILIN I'''
'''REFINED SOLUTION STRUCTURE OF HUMAN PROFILIN I'''
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[[Category: Metzler, W J.]]
[[Category: Metzler, W J.]]
[[Category: Mueller, L.]]
[[Category: Mueller, L.]]
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[[Category: regulatory protein]]
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[[Category: Regulatory protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:01:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:58:57 2008''
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Revision as of 02:01, 3 May 2008

Template:STRUCTURE 1pfl

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 Page seeded by OCA on Sat May 3 05:01:47 2008

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