5t4m
From Proteopedia
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==Crystal Structure of Human Protocadherin-15 EC3-5== | ==Crystal Structure of Human Protocadherin-15 EC3-5== | ||
| - | <StructureSection load='5t4m' size='340' side='right' caption='[[5t4m]], [[Resolution|resolution]] 2.24Å' scene=''> | + | <StructureSection load='5t4m' size='340' side='right'caption='[[5t4m]], [[Resolution|resolution]] 2.24Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5t4m]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T4M OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5t4m]] 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=5T4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T4M 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]] 2.24Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=5t4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t4m OCA], [https://pdbe.org/5t4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t4m RCSB], [https://www.ebi.ac.uk/pdbsum/5t4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t4m ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/PCD15_HUMAN PCD15_HUMAN] Usher syndrome type 1;Autosomal recessive non-syndromic sensorineural deafness type DFNB. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. |
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/PCD15_HUMAN PCD15_HUMAN] Calcium-dependent cell-adhesion protein. Essential for maintenance of normal retinal and cochlear function. |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tip links of the inner ear are protein filaments essential for hearing and balance. Two atypical cadherins, cadherin-23 and protocadherin-15, interact in a Ca(2+)-dependent manner to form tip links. The largely unknown structure and mechanics of these proteins are integral to understanding how tip links pull on ion channels to initiate sensory perception. Protocadherin-15 has 11 extracellular cadherin (EC) repeats. Its EC3-4 linker lacks several of the canonical Ca(2+)-binding residues, and contains an aspartate-to-alanine polymorphism (D414A) under positive selection in East Asian populations. We present structures of protocadherin-15 EC3-5 featuring two Ca(2+)-binding linker regions: canonical EC4-5 linker binding three Ca(2+) ions, and non-canonical EC3-4 linker binding only two Ca(2+) ions. Our structures and biochemical assays reveal little difference between the D414 and D414A variants. Simulations predict that the partial Ca(2+)-free EC3-4 linker exhibits increased flexural flexibility without compromised mechanical strength, providing insight into the dynamics of tip links and other atypical cadherins. | ||
| + | |||
| + | A Partial Calcium-Free Linker Confers Flexibility to Inner-Ear Protocadherin-15.,Powers RE, Gaudet R, Sotomayor M Structure. 2017 Mar 7;25(3):482-495. doi: 10.1016/j.str.2017.01.014. Epub 2017, Feb 23. PMID:28238533<ref>PMID:28238533</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5t4m" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Gaudet R]] |
| - | [[Category: | + | [[Category: Powers RE]] |
| - | [[Category: | + | [[Category: Sotomayor M]] |
| - | + | ||
| - | + | ||
Current revision
Crystal Structure of Human Protocadherin-15 EC3-5
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