2d10
From Proteopedia
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<StructureSection load='2d10' size='340' side='right'caption='[[2d10]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2d10' size='340' side='right'caption='[[2d10]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2d10]] is a 8 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2d10]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D10 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2d10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d10 OCA], [https://pdbe.org/2d10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d10 RCSB], [https://www.ebi.ac.uk/pdbsum/2d10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d10 ProSAT]</span></td></tr> |
</table> | </table> | ||
- | == Disease == | ||
- | [[http://www.uniprot.org/uniprot/NHRF1_HUMAN NHRF1_HUMAN]] Defects in SLC9A3R1 are the cause of hypophosphatemic nephrolithiasis/osteoporosis type 2 (NPHLOP2) [MIM:[http://omim.org/entry/612287 612287]]. Hypophosphatemia results from idiopathic renal phosphate loss. It contributes to the pathogenesis of hypophosphatemic urolithiasis (formation of urinary calculi) as well to that of hypophosphatemic osteoporosis (bone demineralization).<ref>PMID:18784102</ref> <ref>PMID:22506049</ref> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/RADI_MOUSE RADI_MOUSE] Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Mus musculus]] |
- | [[Category: Hakoshima | + | [[Category: Hakoshima T]] |
- | [[Category: Maesaki | + | [[Category: Maesaki R]] |
- | [[Category: Terawaki | + | [[Category: Terawaki S]] |
- | + | ||
- | + |
Current revision
Crystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail peptide
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