1p8z

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[[Image:1p8z.jpg|left|200px]]
 
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{{Structure
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==Complex Between Rabbit Muscle alpha-Actin: Human Gelsolin Residues Val26-Glu156==
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|PDB= 1p8z |SIZE=350|CAPTION= <scene name='initialview01'>1p8z</scene>, resolution 2.60&Aring;
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<StructureSection load='1p8z' size='340' side='right'caption='[[1p8z]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>
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<table><tr><td colspan='2'>[[1p8z]] 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=1P8Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P8Z FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.6&#8491;</td></tr>
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|GENE=
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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=CD:CADMIUM+ION'>CD</scene></td></tr>
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}}
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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=1p8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p8z OCA], [https://pdbe.org/1p8z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p8z RCSB], [https://www.ebi.ac.uk/pdbsum/1p8z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p8z 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/p8/1p8z_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=1p8z ConSurf].
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<div style="clear:both"></div>
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'''Complex Between Rabbit Muscle alpha-Actin: Human Gelsolin Residues Val26-Glu156'''
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==See Also==
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*[[Actin 3D structures|Actin 3D structures]]
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*[[Gelsolin 3D structures|Gelsolin 3D structures]]
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==Overview==
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== References ==
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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.
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<references/>
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__TOC__
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==Disease==
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</StructureSection>
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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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==About this Structure==
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1P8Z is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P8Z OCA].
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==Reference==
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From the first to the second domain of gelsolin: a common path on the surface of actin?, Irobi E, Burtnick LD, Urosev D, Narayan K, Robinson RC, FEBS Lett. 2003 Sep 25;552(2-3):86-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14527665 14527665]
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[[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: Burtnick LD]]
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[[Category: Burtnick, L D.]]
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[[Category: Irobi E]]
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[[Category: Irobi, E.]]
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[[Category: Robinson RC]]
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[[Category: Robinson, R C.]]
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[[Category: ATP]]
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[[Category: CA]]
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[[Category: CD]]
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[[Category: linker between gelsolin domain 1 and domain 2]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:10:53 2008''
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Current revision

Complex Between Rabbit Muscle alpha-Actin: Human Gelsolin Residues Val26-Glu156

PDB ID 1p8z

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