3ud1: Difference between revisions
New page: '''Unreleased structure''' The entry 3ud1 is ON HOLD Authors: Yasunaga, M., Ipsaro, J.J., Mondragon, A. Description: Crystal structure of ZU5A-ZU5B domains of human erythrocyte ankyrin |
No edit summary |
||
(8 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
==Crystal structure of ZU5A-ZU5B domains of human erythrocyte ankyrin== | |||
<StructureSection load='3ud1' size='340' side='right'caption='[[3ud1]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ud1]] is a 3 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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='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> | |||
== 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 == | |||
[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> | |||
==See Also== | |||
*[[Ankyrin 3D structures|Ankyrin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Ipsaro JJ]] | |||
[[Category: Mondragon A]] | |||
[[Category: Yasunaga M]] |