3kbt

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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)==
==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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<StructureSection load='3kbt' size='340' side='right' caption='[[3kbt]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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<StructureSection load='3kbt' size='340' side='right'caption='[[3kbt]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3kbt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KBT FirstGlance]. <br>
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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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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3f57|3f57]], [[3edu|3edu]], [[3edv|3edv]], [[3f59|3f59]], [[1u4q|1u4q]], [[3kbu|3kbu]]</td></tr>
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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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPTB, SPTB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ANK, ANK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kbt OCA], [http://pdbe.org/3kbt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kbt RCSB], [http://www.ebi.ac.uk/pdbsum/3kbt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kbt ProSAT]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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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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[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.
== Function ==
== Function ==
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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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[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kb/3kbt_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Maintenance of membrane integrity and organization in the metazoan cell is accomplished through intracellular tethering of membrane proteins to an extensive, flexible protein network. Spectrin, the principal component of this network, is anchored to membrane proteins through the adaptor protein ankyrin. To elucidate the atomic basis for this interaction, we determined a crystal structure of human betaI-spectrin repeats 13 to 15 in complex with the ZU5-ANK domain of human ankyrin R. The structure reveals the role of repeats 14 to 15 in binding, the electrostatic and hydrophobic contributions along the interface, and the necessity for a particular orientation of the spectrin repeats. Using structural and biochemical data as a guide, we characterized the individual proteins and their interactions by binding and thermal stability analyses. In addition to validating the structural model, these data provide insight into the nature of some mutations associated with cell morphology defects, including those found in human diseases such as hereditary spherocytosis and elliptocytosis. Finally, analysis of the ZU5 domain suggests it is a versatile protein-protein interaction module with distinct interaction surfaces. The structure represents not only the first of a spectrin fragment in complex with its binding partner, but also that of an intermolecular complex involving a ZU5 domain.
 
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Structural basis for spectrin recognition by ankyrin.,Ipsaro JJ, Mondragon A Blood. 2010 May 20;115(20):4093-101. Epub 2010 Jan 25. PMID:20101027<ref>PMID:20101027</ref>
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==See Also==
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*[[Ankyrin 3D structures|Ankyrin 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[Spectrin 3D structures|Spectrin 3D structures]]
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</div>
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<div class="pdbe-citations 3kbt" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[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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