1esv

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(New page: 200px<br /> <applet load="1esv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1esv, resolution 2.0&Aring;" /> '''COMPLEX BETWEEN LATR...)
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[[Image:1esv.gif|left|200px]]<br />
 
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<applet load="1esv" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1esv, resolution 2.0&Aring;" />
 
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'''COMPLEX BETWEEN LATRUNCULIN A:RABBIT MUSCLE ALPHA ACTIN:HUMAN GELSOLIN DOMAIN 1'''<br />
 
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==Disease==
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==COMPLEX BETWEEN LATRUNCULIN A:RABBIT MUSCLE ALPHA ACTIN:HUMAN GELSOLIN DOMAIN 1==
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Known disease associated with this structure: Amyloidosis, Finnish type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=137350 137350]]
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<StructureSection load='1esv' size='340' side='right'caption='[[1esv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1esv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1ESV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ESV FirstGlance]. <br>
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</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>
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<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>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=LAR:LATRUNCULIN+A'>LAR</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1esv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esv OCA], [https://pdbe.org/1esv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1esv RCSB], [https://www.ebi.ac.uk/pdbsum/1esv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1esv ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN] Defects in GSN are the cause of amyloidosis type 5 (AMYL5) [MIM:[https://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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[https://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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/1esv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1esv ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1ESV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with CA, ATP and LAR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ESV OCA].
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*[[Actin 3D structures|Actin 3D structures]]
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*[[Gelsolin 3D structures|Gelsolin 3D structures]]
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==Reference==
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== References ==
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Latrunculin alters the actin-monomer subunit interface to prevent polymerization., Morton WM, Ayscough KR, McLaughlin PJ, Nat Cell Biol. 2000 Jun;2(6):376-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10854330 10854330]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Protein complex]]
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[[Category: Ayscough KA]]
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[[Category: Ayscough, K.A.]]
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[[Category: McLaughlin PJ]]
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[[Category: McLaughlin, P.J.]]
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[[Category: Morton WM]]
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[[Category: Morton, W.M.]]
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[[Category: ATP]]
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[[Category: CA]]
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[[Category: LAR]]
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[[Category: actin]]
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[[Category: depolymerisation]]
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[[Category: gelsolin]]
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[[Category: latrunculin a]]
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[[Category: sequestration]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:46:29 2007''
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Current revision

COMPLEX BETWEEN LATRUNCULIN A:RABBIT MUSCLE ALPHA ACTIN:HUMAN GELSOLIN DOMAIN 1

PDB ID 1esv

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