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[[Image:1t44.gif|left|200px]]<br /><applet load="1t44" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1t44, resolution 2.00&Aring;" />
'''Structural basis of actin sequestration by thymosin-B4: Implications for arp2/3 activation'''<br />


==Overview==
==Structural basis of actin sequestration by thymosin-B4: Implications for arp2/3 activation==
<StructureSection load='1t44' size='340' side='right'caption='[[1t44]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1t44]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T44 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t44 OCA], [https://pdbe.org/1t44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t44 RCSB], [https://www.ebi.ac.uk/pdbsum/1t44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t44 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t4/1t44_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t44 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
Structural basis of actin sequestration by thymosin-beta4: implications for WH2 proteins.,Irobi E, Aguda AH, Larsson M, Guerin C, Yin HL, Burtnick LD, Blanchoin L, Robinson RC EMBO J. 2004 Sep 15;23(18):3599-608. Epub 2004 Aug 26. PMID:15329672<ref>PMID:15329672</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1T44 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens,_mus_musculus Homo sapiens, mus musculus] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T44 OCA].
</div>
<div class="pdbe-citations 1t44" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural basis of actin sequestration by thymosin-beta4: implications for WH2 proteins., Irobi E, Aguda AH, Larsson M, Guerin C, Yin HL, Burtnick LD, Blanchoin L, Robinson RC, EMBO J. 2004 Sep 15;23(18):3599-608. Epub 2004 Aug 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15329672 15329672]
*[[Actin 3D structures|Actin 3D structures]]
[[Category: Homo sapiens, mus musculus]]
*[[Gelsolin 3D structures|Gelsolin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Protein complex]]
[[Category: Aguda AH]]
[[Category: Aguda, A H.]]
[[Category: Burtnick LD]]
[[Category: Burtnick, L D.]]
[[Category: Irobi E]]
[[Category: Irobi, E.]]
[[Category: Larsson M]]
[[Category: Larsson, M.]]
[[Category: Robinson RC]]
[[Category: Robinson, R C.]]
[[Category: ATP]]
[[Category: CA]]
[[Category: structural protein]]
 
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Retrieved from "https://proteopedia.org/1t44"