2prf
From Proteopedia
(New page: 200px<br /><applet load="2prf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2prf" /> '''THREE DIMENSIONAL SOLUTION STRUCTURE OF ACAN...) |
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| - | [[Image:2prf.gif|left|200px]]<br /><applet load="2prf" size=" | + | [[Image:2prf.gif|left|200px]]<br /><applet load="2prf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2prf" /> | caption="2prf" /> | ||
'''THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I'''<br /> | '''THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined a medium resolution three-dimensional solution | + | 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 Structure== | ==About this Structure== | ||
| - | 2PRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_sp. Acanthamoeba sp.]. Full crystallographic information is available from [http:// | + | 2PRF is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Acanthamoeba sp.]] | [[Category: Acanthamoeba sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Archer, S | + | [[Category: Archer, S J.]] |
| - | [[Category: Lattman, E | + | [[Category: Lattman, E E.]] |
| - | [[Category: Pollard, T | + | [[Category: Pollard, T D.]] |
| - | [[Category: Torchia, D | + | [[Category: Torchia, D A.]] |
| - | [[Category: Vinson, V | + | [[Category: Vinson, V K.]] |
[[Category: actin-binding]] | [[Category: actin-binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:32:15 2008'' |
Revision as of 16:32, 21 February 2008
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THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I
Overview
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 Structure
2PRF is a Single protein structure of sequence from Acanthamoeba sp.. Full crystallographic information is available from OCA.
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:8397216
Page seeded by OCA on Thu Feb 21 18:32:15 2008
