2yvi: Difference between revisions
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<StructureSection load='2yvi' size='340' side='right'caption='[[2yvi]], [[Resolution|resolution]] 1.92Å' scene=''> | <StructureSection load='2yvi' size='340' side='right'caption='[[2yvi]], [[Resolution|resolution]] 1.92Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2yvi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92Å</td></tr> | ||
<tr id=' | <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> | ||
<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> | <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> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
[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> | |||
== Function == | == Function == | ||
[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> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bessho | [[Category: Bessho Y]] | ||
[[Category: Chen | [[Category: Chen L]] | ||
[[Category: Ihsanawati]] | [[Category: Ihsanawati]] | ||
[[Category: Liu | [[Category: Liu ZJ]] | ||
[[Category: Shirouzu M]] | |||
[[Category: Shirouzu | [[Category: Wang BC]] | ||
[[Category: Wang | [[Category: Yokoyama S]] | ||
[[Category: Yokoyama | |||
Latest revision as of 16:55, 13 March 2024
Crystal structure of a death domain of human ankryn proteinCrystal structure of a death domain of human ankryn protein
Structural highlights
DiseaseANK1_HUMAN Defects in ANK1 are a cause of spherocytosis type 1 (SPH1) [MIM: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.[1] [2] FunctionANK1_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.[3] Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils.[4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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