1n11

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{{STRUCTURE_1n11| PDB=1n11 | SCENE= }}
 
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===D34 REGION OF HUMAN ANKYRIN-R AND LINKER===
 
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{{ABSTRACT_PUBMED_12456646}}
 
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==Disease==
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==D34 REGION OF HUMAN ANKYRIN-R AND LINKER==
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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='1n11' size='340' side='right'caption='[[1n11]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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==Function==
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<table><tr><td colspan='2'>[[1n11]] 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=1N11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N11 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]] 2.7&#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=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=1n11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n11 OCA], [https://pdbe.org/1n11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n11 RCSB], [https://www.ebi.ac.uk/pdbsum/1n11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n11 ProSAT]</span></td></tr>
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[[1n11]] 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=1N11 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/n1/1n11_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=1n11 ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
*[[Ankyrin|Ankyrin]]
*[[Ankyrin|Ankyrin]]
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*[[Ankyrin 3D structures|Ankyrin 3D structures]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:012456646</ref><references group="xtra"/><references/>
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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: Anderson, R G.W.]]
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[[Category: Large Structures]]
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[[Category: Machius, M.]]
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[[Category: Anderson RGW]]
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[[Category: Michaely, P.]]
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[[Category: Machius M]]
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[[Category: Tomchick, D R.]]
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[[Category: Michaely P]]
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[[Category: Anion exchanger]]
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[[Category: Tomchick DR]]
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[[Category: Ankyrin]]
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[[Category: Band 3]]
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[[Category: Clathrin]]
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[[Category: Structural protein]]
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Current revision

D34 REGION OF HUMAN ANKYRIN-R AND LINKER

PDB ID 1n11

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