1p8z: Difference between revisions

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==Overview==

We present the 2.6 A resolution crystal structure of a complex formed, between G-actin and gelsolin fragment Met25-Gln160 (G1+). The structure, differs from those of other gelsolin domain 1 (G1) complexes in that an, additional six amino acid residues from the crucial linker region into, gelsolin domain 2 (G2) are visible and are attached securely to the, surface of actin. The linker segment extends away from G1 up the face of, actin in a direction that infers G2 will bind along the same long-pitch, helical strand as the actin bound to G1. This is consistent with a, mechanism whereby G2 attaches gelsolin to the side of a filament and then, directs G1 toward a position where it would disrupt actin-actin contacts., Alignment of the sequence of the structurally important residues within, the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein, family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin, beta4) suggests that the opposing activities of filament assembly and, disassembly may exploit a common patch on the surface of actin.

We present the 2.6 A resolution crystal structure of a complex formed between G-actin and gelsolin fragment Met25-Gln160 (G1+). The structure differs from those of other gelsolin domain 1 (G1) complexes in that an additional six amino acid residues from the crucial linker region into gelsolin domain 2 (G2) are visible and are attached securely to the surface of actin. The linker segment extends away from G1 up the face of actin in a direction that infers G2 will bind along the same long-pitch helical strand as the actin bound to G1. This is consistent with a mechanism whereby G2 attaches gelsolin to the side of a filament and then directs G1 toward a position where it would disrupt actin-actin contacts. Alignment of the sequence of the structurally important residues within the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin beta4) suggests that the opposing activities of filament assembly and disassembly may exploit a common patch on the surface of actin.

==Disease==

Line 17:

[[Category: Oryctolagus cuniculus]]

[[Category: Protein complex]]

[[Category: Burtnick, L.D.]]

[[Category: Burtnick, L D.]]

[[Category: Irobi, E.]]

[[Category: Robinson, R.C.]]

[[Category: Robinson, R C.]]

[[Category: ATP]]

[[Category: CA]]

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[[Category: linker between gelsolin domain 1 and domain 2]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-We present the 2.6 A resolution crystal structure of a complex formed, between G-actin and gelsolin fragment Met25-Gln160 (G1+). The structure, differs from those of other gelsolin domain 1 (G1) complexes in that an, additional six amino acid residues from the crucial linker region into, gelsolin domain 2 (G2) are visible and are attached securely to the, surface of actin. The linker segment extends away from G1 up the face of, actin in a direction that infers G2 will bind along the same long-pitch, helical strand as the actin bound to G1. This is consistent with a, mechanism whereby G2 attaches gelsolin to the side of a filament and then, directs G1 toward a position where it would disrupt actin-actin contacts., Alignment of the sequence of the structurally important residues within, the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein, family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin, beta4) suggests that the opposing activities of filament assembly and, disassembly may exploit a common patch on the surface of actin.
+We present the 2.6 A resolution crystal structure of a complex formed between G-actin and gelsolin fragment Met25-Gln160 (G1+). The structure differs from those of other gelsolin domain 1 (G1) complexes in that an additional six amino acid residues from the crucial linker region into gelsolin domain 2 (G2) are visible and are attached securely to the surface of actin. The linker segment extends away from G1 up the face of actin in a direction that infers G2 will bind along the same long-pitch helical strand as the actin bound to G1. This is consistent with a mechanism whereby G2 attaches gelsolin to the side of a filament and then directs G1 toward a position where it would disrupt actin-actin contacts. Alignment of the sequence of the structurally important residues within the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin beta4) suggests that the opposing activities of filament assembly and disassembly may exploit a common patch on the surface of actin.
 ==Disease==
@@ Line 17: / Line 17: @@
 [[Category: Oryctolagus cuniculus]]
 [[Category: Protein complex]]
-[[Category: Burtnick, L.D.]]
+[[Category: Burtnick, L D.]]
 [[Category: Irobi, E.]]
-[[Category: Robinson, R.C.]]
+[[Category: Robinson, R C.]]
 [[Category: ATP]]
 [[Category: CA]]
@@ Line 25: / Line 25: @@
 [[Category: linker between gelsolin domain 1 and domain 2]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:39:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:29 2008''