1t44: Difference between revisions

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|PDB= 1t44 |SIZE=350|CAPTION= <scene name='initialview01'>1t44</scene>, resolution 2.00&Aring;
|PDB= 1t44 |SIZE=350|CAPTION= <scene name='initialview01'>1t44</scene>, resolution 2.00&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>
|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[1p8z|1P8Z]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t44 OCA], [http://www.ebi.ac.uk/pdbsum/1t44 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t44 RCSB]</span>
}}
}}


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==Overview==
==Overview==
The WH2 (Wiscott-Aldridge syndrome protein homology domain 2) repeat is an actin interacting motif found in monomer sequestering and filament assembly proteins. We have stabilized the prototypical WH2 family member, thymosin-beta4 (Tbeta4), with respect to actin, by creating a hybrid between gelsolin domain 1 and the C-terminal half of Tbeta4 (G1-Tbeta4). This hybrid protein sequesters actin monomers, severs actin filaments and acts as a leaky barbed end cap. Here, we present the structure of the G1-Tbeta4:actin complex at 2 A resolution. The structure reveals that Tbeta4 sequesters by capping both ends of the actin monomer, and that exchange of actin between Tbeta4 and profilin is mediated by a minor overlap in binding sites. The structure implies that multiple WH2 motif-containing proteins will associate longitudinally with actin filaments. Finally, we discuss the role of the WH2 motif in arp2/3 activation.
The WH2 (Wiscott-Aldridge syndrome protein homology domain 2) repeat is an actin interacting motif found in monomer sequestering and filament assembly proteins. We have stabilized the prototypical WH2 family member, thymosin-beta4 (Tbeta4), with respect to actin, by creating a hybrid between gelsolin domain 1 and the C-terminal half of Tbeta4 (G1-Tbeta4). This hybrid protein sequesters actin monomers, severs actin filaments and acts as a leaky barbed end cap. Here, we present the structure of the G1-Tbeta4:actin complex at 2 A resolution. The structure reveals that Tbeta4 sequesters by capping both ends of the actin monomer, and that exchange of actin between Tbeta4 and profilin is mediated by a minor overlap in binding sites. The structure implies that multiple WH2 motif-containing proteins will associate longitudinally with actin filaments. Finally, we discuss the role of the WH2 motif in arp2/3 activation.
==Disease==
Known diseases associated with this structure: Myopathy, actin, congenital, with cores OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=102610 102610]], Myopathy, actin, congenital, with excess of thin myofilaments OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=102610 102610]], Myopathy, congenital, with fiber-type disporportion 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=102610 102610]], Myopathy, nemaline, 3 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=102610 102610]]


==About this Structure==
==About this Structure==
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[[Category: Larsson, M.]]
[[Category: Larsson, M.]]
[[Category: Robinson, R C.]]
[[Category: Robinson, R C.]]
[[Category: ATP]]
[[Category: CA]]
[[Category: structural protein]]
[[Category: structural protein]]


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