2acg: Difference between revisions

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[[Image:2acg.gif|left|200px]]<br /><applet load="2acg" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2acg.gif|left|200px]]<br /><applet load="2acg" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2acg, resolution 2.5Å" />

'''ACANTHAMOEBA CASTELLANII PROFILIN II'''<br />

==Overview==

We determined the structures of Acanthamoeba profilin I and profilin II by, x-ray crystallography at resolutions of 2.0 and 2.8 A, respectively. The, polypeptide folds and the actin-binding surfaces of the amoeba profilins, are very similar to those of bovine and human profilins. The electrostatic, potential surfaces of the two Acanthamoeba isoforms differ. Two areas of, high positive potential on the surface of profilin II are candidate, binding sites for phosphatidylinositol phosphates. The proximity of these, sites to the actin binding site provides an explanation for the, competition between actin and lipids for binding profilin.

We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 A, respectively. The polypeptide folds and the actin-binding surfaces of the amoeba profilins are very similar to those of bovine and human profilins. The electrostatic potential surfaces of the two Acanthamoeba isoforms differ. Two areas of high positive potential on the surface of profilin II are candidate binding sites for phosphatidylinositol phosphates. The proximity of these sites to the actin binding site provides an explanation for the competition between actin and lipids for binding profilin.

==About this Structure==

2ACG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2ACG OCA].

2ACG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ACG OCA].

==Reference==

Line 13:

[[Category: Acanthamoeba castellanii]]

[[Category: Single protein]]

[[Category: Almo, S.C.]]

[[Category: Almo, S C.]]

[[Category: Fedorov, A.A.]]

[[Category: Fedorov, A A.]]

[[Category: Graupe, M.H.]]

[[Category: Graupe, M H.]]

[[Category: Lattman, E.E.]]

[[Category: Lattman, E E.]]

[[Category: Magnus, K.A.]]

[[Category: Magnus, K A.]]

[[Category: Pollard, T.D.]]

[[Category: Pollard, T D.]]

[[Category: actin-binding protein]]

[[Category: profilin]]

[[Category: protein binding]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 08:02:~~54 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:25:59 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2acg.gif|left|200px]]<br /><applet load="2acg" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2acg.gif|left|200px]]<br /><applet load="2acg" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2acg, resolution 2.5&Aring;" />
 '''ACANTHAMOEBA CASTELLANII PROFILIN II'''<br />
 ==Overview==
-We determined the structures of Acanthamoeba profilin I and profilin II by, x-ray crystallography at resolutions of 2.0 and 2.8 A, respectively. The, polypeptide folds and the actin-binding surfaces of the amoeba profilins, are very similar to those of bovine and human profilins. The electrostatic, potential surfaces of the two Acanthamoeba isoforms differ. Two areas of, high positive potential on the surface of profilin II are candidate, binding sites for phosphatidylinositol phosphates. The proximity of these, sites to the actin binding site provides an explanation for the, competition between actin and lipids for binding profilin.
+We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 A, respectively. The polypeptide folds and the actin-binding surfaces of the amoeba profilins are very similar to those of bovine and human profilins. The electrostatic potential surfaces of the two Acanthamoeba isoforms differ. Two areas of high positive potential on the surface of profilin II are candidate binding sites for phosphatidylinositol phosphates. The proximity of these sites to the actin binding site provides an explanation for the competition between actin and lipids for binding profilin.
 ==About this Structure==
-ACG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ACG OCA].
+ACG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ACG OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Acanthamoeba castellanii]]
 [[Category: Single protein]]
-[[Category: Almo, S.C.]]
+[[Category: Almo, S C.]]
-[[Category: Fedorov, A.A.]]
+[[Category: Fedorov, A A.]]
-[[Category: Graupe, M.H.]]
+[[Category: Graupe, M H.]]
-[[Category: Lattman, E.E.]]
+[[Category: Lattman, E E.]]
-[[Category: Magnus, K.A.]]
+[[Category: Magnus, K A.]]
-[[Category: Pollard, T.D.]]
+[[Category: Pollard, T D.]]
 [[Category: actin-binding protein]]
 [[Category: profilin]]
 [[Category: protein binding]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:02:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:25:59 2008''