4z94

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'''Unreleased structure'''
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==Actin Complex With a Chimera of Tropomodulin-1 and Leiomodin-1 Actin-Binding Site 2==
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<StructureSection load='4z94' size='340' side='right' caption='[[4z94]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4z94]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z94 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z94 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4z8g|4z8g]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4z94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z94 OCA], [http://pdbe.org/4z94 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z94 RCSB], [http://www.ebi.ac.uk/pdbsum/4z94 PDBsum]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN]] Defects in GSN are the cause of amyloidosis type 5 (AMYL5) [MIM:[http://omim.org/entry/105120 105120]]; also known as familial amyloidosis Finnish type. AMYL5 is a hereditary generalized amyloidosis due to gelsolin amyloid deposition. It is typically characterized by cranial neuropathy and lattice corneal dystrophy. Most patients have modest involvement of internal organs, but severe systemic disease can develop in some individuals causing peripheral polyneuropathy, amyloid cardiomyopathy, and nephrotic syndrome leading to renal failure.<ref>PMID:2157434</ref> <ref>PMID:2153578</ref> <ref>PMID:2176481</ref> <ref>PMID:1338910</ref>
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== Function ==
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[[http://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. [[http://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN]] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.<ref>PMID:20393563</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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How proteins sharing a common fold have evolved different functions is a fundamental question in biology. Tropomodulins (Tmods) are prototypical actin filament pointed-end-capping proteins, whereas their homologues, Leiomodins (Lmods), are powerful filament nucleators. We show that Tmods and Lmods do not compete biochemically, and display similar but distinct localization in sarcomeres. Changes along the polypeptide chains of Tmods and Lmods exquisitely adapt their functions for capping versus nucleation. Tmods have alternating tropomyosin (TM)- and actin-binding sites (TMBS1, ABS1, TMBS2 and ABS2). Lmods additionally contain a C-terminal extension featuring an actin-binding WH2 domain. Unexpectedly, the different activities of Tmods and Lmods do not arise from the Lmod-specific extension. Instead, nucleation by Lmods depends on two major adaptations-the loss of pointed-end-capping elements present in Tmods and the specialization of the highly conserved ABS2 for recruitment of two or more actin subunits. The WH2 domain plays only an auxiliary role in nucleation.
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The entry 4z94 is ON HOLD until Paper Publication
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How Leiomodin and Tropomodulin use a common fold for different actin assembly functions.,Boczkowska M, Rebowski G, Kremneva E, Lappalainen P, Dominguez R Nat Commun. 2015 Sep 15;6:8314. doi: 10.1038/ncomms9314. PMID:26370058<ref>PMID:26370058</ref>
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Authors: Rebowski, G., Boczkowska, M., Dominguez, R.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Actin Complex With a Chimera of Tropomodulin-1 and Leiomodin-1 Actin-Binding Site 2
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<div class="pdbe-citations 4z94" style="background-color:#fffaf0;"></div>
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[[Category: Unreleased Structures]]
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== References ==
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[[Category: Rebowski, G]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Oryctolagus cuniculus]]
[[Category: Boczkowska, M]]
[[Category: Boczkowska, M]]
[[Category: Dominguez, R]]
[[Category: Dominguez, R]]
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[[Category: Rebowski, G]]
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[[Category: Actin nucleator]]
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[[Category: Atp-actin]]
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[[Category: Protein binding-structural protein complex]]

Revision as of 05:26, 22 October 2015

Actin Complex With a Chimera of Tropomodulin-1 and Leiomodin-1 Actin-Binding Site 2

4z94, resolution 2.40Å

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