2prf: Difference between revisions
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[[Image:2prf.gif|left|200px]] | [[Image:2prf.gif|left|200px]] | ||
'''THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I''' | {{Structure | ||
|PDB= 2prf |SIZE=350|CAPTION= <scene name='initialview01'>2prf</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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'''THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2PRF is a [ | 2PRF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_sp. Acanthamoeba sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRF OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8397216 8397216] | ||
[[Category: Acanthamoeba sp.]] | [[Category: Acanthamoeba sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: actin-binding]] | [[Category: actin-binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:16:30 2008'' | ||
Revision as of 19:16, 20 March 2008
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THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I
OverviewOverview
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.
About this StructureAbout this Structure
2PRF is a Single protein structure of sequence from Acanthamoeba sp.. Full crystallographic information is available from OCA.
ReferenceReference
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
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