3kbt

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{{STRUCTURE_3kbt| PDB=3kbt | SCENE= }}
 
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===Crystal structure of the ankyrin binding domain of human erythroid beta spectrin (repeats 13-15) in complex with the spectrin binding domain of human erythroid ankyrin (ZU5-ANK)===
 
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{{ABSTRACT_PUBMED_20101027}}
 
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==Disease==
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==Crystal structure of the ankyrin binding domain of human erythroid beta spectrin (repeats 13-15) in complex with the spectrin binding domain of human erythroid ankyrin (ZU5-ANK)==
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[[http://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN]] Defects in SPTB are the cause of elliptocytosis type 3 (EL3) [MIM:[http://omim.org/entry/182870 182870]]. EL3 is a Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape.<ref>PMID:8226774</ref><ref>PMID:7883966</ref><ref>PMID:8018926</ref><ref>PMID:1975598</ref> Defects in SPTB are the cause of spherocytosis type 2 (SPH2) [MIM:[http://omim.org/entry/182870 182870]]; also known as hereditary spherocytosis type 2 (HS2). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH2 is characterized by severe hemolytic anemia. Inheritance is autosomal dominant. [[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='3kbt' size='340' side='right'caption='[[3kbt]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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== Structural highlights ==
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==Function==
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<table><tr><td colspan='2'>[[3kbt]] is a 4 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=3KBT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KBT FirstGlance]. <br>
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[[http://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN]] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. [[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]] 2.75&#8491;</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=3kbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kbt OCA], [https://pdbe.org/3kbt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kbt RCSB], [https://www.ebi.ac.uk/pdbsum/3kbt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kbt ProSAT]</span></td></tr>
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==About this Structure==
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</table>
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[[3kbt]] is a 4 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=3KBT OCA].
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== Disease ==
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[https://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN] Defects in SPTB are the cause of elliptocytosis type 3 (EL3) [MIM:[https://omim.org/entry/182870 182870]. EL3 is a Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape.<ref>PMID:8226774</ref> <ref>PMID:7883966</ref> <ref>PMID:8018926</ref> <ref>PMID:1975598</ref> Defects in SPTB are the cause of spherocytosis type 2 (SPH2) [MIM:[https://omim.org/entry/182870 182870]; also known as hereditary spherocytosis type 2 (HS2). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH2 is characterized by severe hemolytic anemia. Inheritance is autosomal dominant.
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== Function ==
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[https://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
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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/kb/3kbt_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=3kbt 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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*[[Spectrin 3D structures|Spectrin 3D structures]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:020101027</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: Ipsaro, J J.]]
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[[Category: Large Structures]]
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[[Category: Mondragon, A.]]
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[[Category: Ipsaro JJ]]
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[[Category: Actin capping]]
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[[Category: Mondragon A]]
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[[Category: Actin-binding]]
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[[Category: Alternative promoter usage]]
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[[Category: Ank repeat]]
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[[Category: Ankyrin]]
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[[Category: Ankyrin binding]]
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[[Category: Beta sandwich]]
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[[Category: Complex]]
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[[Category: Cytoskeleton]]
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[[Category: Disease mutation]]
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[[Category: Elliptocytosis]]
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[[Category: Hereditary hemolytic anemia]]
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[[Category: Lipoprotein]]
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[[Category: Membrane]]
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[[Category: Membrane skeleton]]
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[[Category: Phosphoprotein]]
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[[Category: Sarcoplasmic reticulum]]
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[[Category: Spectrin]]
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[[Category: Spectrin binding]]
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[[Category: Spectrin repeat]]
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[[Category: Structural protein]]
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[[Category: Three helix bundle]]
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[[Category: Zu5]]
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Current revision

Crystal structure of the ankyrin binding domain of human erythroid beta spectrin (repeats 13-15) in complex with the spectrin binding domain of human erythroid ankyrin (ZU5-ANK)

PDB ID 3kbt

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