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3qij

From Proteopedia

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'''Unreleased structure'''
 
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The entry 3qij is ON HOLD
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==Primitive-monoclinic crystal structure of the FERM domain of protein 4.1R==
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<StructureSection load='3qij' size='340' side='right'caption='[[3qij]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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Authors: Nedyalkova, L., Zhong, N., Tong, Y., Tempel, W., Arrowsmith, C.H., Edwards, A.M., Bountra, C., Weigelt, J., Park, H., Structural Genomics Consortium (SGC)
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3qij]] is a 2 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=3QIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QIJ FirstGlance]. <br>
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Description: Primitive-monoclinic crystal structure of the FERM domain of protein 4.1R
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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]] 1.8&#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=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></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=3qij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qij OCA], [https://pdbe.org/3qij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qij RCSB], [https://www.ebi.ac.uk/pdbsum/3qij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qij ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/EPB41_HUMAN EPB41_HUMAN] Hereditary elliptocytosis. The disease is caused by variants affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/EPB41_HUMAN EPB41_HUMAN] Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase (PubMed:23870127).<ref>PMID:23870127</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra C]]
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[[Category: Edwards AM]]
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[[Category: Nedyalkova L]]
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[[Category: Park H]]
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[[Category: Tempel W]]
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[[Category: Tong Y]]
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[[Category: Weigelt J]]
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[[Category: Zhong N]]

Current revision

Primitive-monoclinic crystal structure of the FERM domain of protein 4.1R

PDB ID 3qij

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OCA

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