2yvi

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{{STRUCTURE_2yvi| PDB=2yvi | SCENE= }}
 
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===Crystal structure of a death domain of human ankryn protein===
 
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==Disease==
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==Crystal structure of a death domain of human ankryn protein==
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[[http://www.uniprot.org/uniprot/ANK1_HUMAN ANK1_HUMAN]] Defects in ANK1 are a cause of spherocytosis type 1 (SPH1) [MIM:[http://omim.org/entry/182900 182900]]; also called hereditary spherocytosis type 1 (HS1). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Inheritance can be autosomal dominant or recessive.<ref>PMID:8640229</ref><ref>PMID:11102985</ref>
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<StructureSection load='2yvi' size='340' side='right'caption='[[2yvi]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
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== Structural highlights ==
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==Function==
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<table><tr><td colspan='2'>[[2yvi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YVI FirstGlance]. <br>
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[[http://www.uniprot.org/uniprot/ANK1_HUMAN ANK1_HUMAN]] Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions.<ref>PMID:12456646</ref> Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils.<ref>PMID:12456646</ref>
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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]] 1.92&#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=GOL:GLYCEROL'>GOL</scene></td></tr>
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==About this Structure==
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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=2yvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yvi OCA], [https://pdbe.org/2yvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yvi RCSB], [https://www.ebi.ac.uk/pdbsum/2yvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yvi ProSAT], [https://www.topsan.org/Proteins/RSGI/2yvi TOPSAN]</span></td></tr>
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[[2yvi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YVI OCA].
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ANK1_HUMAN ANK1_HUMAN] Defects in ANK1 are a cause of spherocytosis type 1 (SPH1) [MIM:[https://omim.org/entry/182900 182900]; also called hereditary spherocytosis type 1 (HS1). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Inheritance can be autosomal dominant or recessive.<ref>PMID:8640229</ref> <ref>PMID:11102985</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/ANK1_HUMAN ANK1_HUMAN] Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions.<ref>PMID:12456646</ref> Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils.<ref>PMID:12456646</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/yv/2yvi_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=2yvi ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Ankyrin|Ankyrin]]
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*[[Ankyrin 3D structures|Ankyrin 3D structures]]
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== References ==
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==Reference==
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<references/>
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<references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bessho, Y.]]
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[[Category: Large Structures]]
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[[Category: Chen, L.]]
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[[Category: Bessho Y]]
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[[Category: Chen L]]
[[Category: Ihsanawati]]
[[Category: Ihsanawati]]
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[[Category: Liu, Z J.]]
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[[Category: Liu ZJ]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
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[[Category: Shirouzu M]]
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[[Category: Shirouzu, M.]]
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[[Category: Wang BC]]
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[[Category: Wang, B C.]]
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[[Category: Yokoyama S]]
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[[Category: Yokoyama, S.]]
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[[Category: Cell adhesion]]
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[[Category: Death domain]]
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[[Category: Homo sapien]]
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[[Category: Monomer]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Riken structural genomics/proteomics initiative]]
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[[Category: Rsgi]]
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[[Category: Structural genomic]]
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Current revision

Crystal structure of a death domain of human ankryn protein

PDB ID 2yvi

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