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| | ==Crystal structure of ZU5A-ZU5B domains of human erythrocyte ankyrin== | | ==Crystal structure of ZU5A-ZU5B domains of human erythrocyte ankyrin== |
| - | <StructureSection load='3ud1' size='340' side='right' caption='[[3ud1]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3ud1' size='340' side='right'caption='[[3ud1]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ud1]] is a 3 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=3UD1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UD1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ud1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UD1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ud2|3ud2]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ud2|3ud2]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ANK1, ANK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ANK1, ANK ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <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=3ud1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ud1 OCA], [http://pdbe.org/3ud1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ud1 RCSB], [http://www.ebi.ac.uk/pdbsum/3ud1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ud1 ProSAT]</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=3ud1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ud1 OCA], [https://pdbe.org/3ud1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ud1 RCSB], [https://www.ebi.ac.uk/pdbsum/3ud1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ud1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[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> | + | [[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 == |
| - | [[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> | + | [[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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Ankyrin|Ankyrin]] | + | *[[Ankyrin 3D structures|Ankyrin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Human]] | | [[Category: Human]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Ipsaro, J J]] | | [[Category: Ipsaro, J J]] |
| | [[Category: Mondragon, A]] | | [[Category: Mondragon, A]] |
| Structural highlights
Disease
[ANK1_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]
Function
[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.[3] Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils.[4]
Publication Abstract from PubMed
The metazoan cell membrane is highly organized. Maintaining such organization and preserving membrane integrity under different conditions are accomplished through intracellular tethering to an extensive, flexible protein network. Spectrin, the principal component of this network, is attached to the membrane through the adaptor protein ankyrin, which directly bridges the interaction between beta-spectrin and membrane proteins. Ankyrins have a modular structure that includes two tandem ZU5 domains. The first domain, ZU5A, is directly responsible for binding beta-spectrin. Here, we present a structure of the tandem ZU5 repeats of human erythrocyte ankyrin. Structural and biophysical experiments show that the second ZU5 domain, ZU5B, does not participate in spectrin binding. ZU5B is structurally similar to the ZU5 domain found in the netrin receptor UNC5b supramodule, suggesting that it could interact with other domains in ankyrin. Comparison of several ZU5 domains demonstrates that the ZU5 domain represents a compact and versatile protein interaction module.
Structurally Similar but Functionally Diverse ZU5 Domains in Human Erythrocyte Ankyrin.,Yasunaga M, Ipsaro JJ, Mondragon A J Mol Biol. 2012 Jan 30. PMID:22310050[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Eber SW, Gonzalez JM, Lux ML, Scarpa AL, Tse WT, Dornwell M, Herbers J, Kugler W, Ozcan R, Pekrun A, Gallagher PG, Schroter W, Forget BG, Lux SE. Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis. Nat Genet. 1996 Jun;13(2):214-8. PMID:8640229 doi:10.1038/ng0696-214
- ↑ Leite RC, Basseres DS, Ferreira JS, Alberto FL, Costa FF, Saad ST. Low frequency of ankyrin mutations in hereditary spherocytosis: identification of three novel mutations. Hum Mutat. 2000 Dec;16(6):529. PMID:11102985 doi:<529::AID-HUMU13>3.0.CO;2-N 10.1002/1098-1004(200012)16:6<529::AID-HUMU13>3.0.CO;2-N
- ↑ Michaely P, Tomchick DR, Machius M, Anderson RG. Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO J. 2002 Dec 2;21(23):6387-96. PMID:12456646
- ↑ Michaely P, Tomchick DR, Machius M, Anderson RG. Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO J. 2002 Dec 2;21(23):6387-96. PMID:12456646
- ↑ Yasunaga M, Ipsaro JJ, Mondragon A. Structurally Similar but Functionally Diverse ZU5 Domains in Human Erythrocyte Ankyrin. J Mol Biol. 2012 Jan 30. PMID:22310050 doi:http://dx.doi.org/10.1016/j.jmb.2012.01.041
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