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| | <StructureSection load='6mfo' size='340' side='right'caption='[[6mfo]], [[Resolution|resolution]] 3.15Å' scene=''> | | <StructureSection load='6mfo' size='340' side='right'caption='[[6mfo]], [[Resolution|resolution]] 3.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mfo]] is a 1 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=6MFO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6MFO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mfo]] is a 1 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=6MFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MFO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.15Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PCDH15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6mfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mfo OCA], [http://pdbe.org/6mfo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mfo RCSB], [http://www.ebi.ac.uk/pdbsum/6mfo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mfo 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=6mfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mfo OCA], [https://pdbe.org/6mfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mfo RCSB], [https://www.ebi.ac.uk/pdbsum/6mfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mfo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == 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 == |
| | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6mfo" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6mfo" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Cadherin 3D structures|Cadherin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Choudhary, D]] | + | [[Category: Choudhary D]] |
| - | [[Category: Sotomayor, M]] | + | [[Category: Sotomayor M]] |
| - | [[Category: Calcium-binding protein]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Hair cell]]
| + | |
| - | [[Category: Mechanotransduction]]
| + | |
| - | [[Category: Stereocilia]]
| + | |
| - | [[Category: Tip link]]
| + | |
| Structural highlights
Disease
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
PCD15_HUMAN Calcium-dependent cell-adhesion protein. Essential for maintenance of normal retinal and cochlear function.
Publication Abstract from PubMed
The vertebrate inner ear, responsible for hearing and balance, is able to sense minute mechanical stimuli originating from an extraordinarily broad range of sound frequencies and intensities or from head movements. Integral to these processes is the tip-link protein complex, which conveys force to open the inner-ear transduction channels that mediate sensory perception. Protocadherin-15 and cadherin-23, two atypically large cadherins with 11 and 27 extracellular cadherin (EC) repeats, are involved in deafness and balance disorders and assemble as parallel homodimers that interact to form the tip link. Here we report the X-ray crystal structure of a protocadherin-15 + cadherin-23 heterotetrameric complex at 2.9-A resolution, depicting a parallel homodimer of protocadherin-15 EC1-3 molecules forming an antiparallel complex with two cadherin-23 EC1-2 molecules. In addition, we report structures for 10 protocadherin-15 fragments used to build complete high-resolution models of the monomeric protocadherin-15 ectodomain. Molecular dynamics simulations and validated crystal contacts are used to propose models for the complete extracellular protocadherin-15 parallel homodimer and the tip-link bond. Steered molecular dynamics simulations of these models suggest conditions in which a structurally diverse and multimodal protocadherin-15 ectodomain can act as a stiff or soft gating spring. These results reveal the structural determinants of tip-link-mediated inner-ear sensory perception and elucidate protocadherin-15's structural and adhesive properties relevant in disease.
Structural determinants of protocadherin-15 mechanics and function in hearing and balance perception.,Choudhary D, Narui Y, Neel BL, Wimalasena LN, Klanseck CF, De-la-Torre P, Chen C, Araya-Secchi R, Tamilselvan E, Sotomayor M Proc Natl Acad Sci U S A. 2020 Sep 22. pii: 1920444117. doi:, 10.1073/pnas.1920444117. PMID:32963095[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Choudhary D, Narui Y, Neel BL, Wimalasena LN, Klanseck CF, De-la-Torre P, Chen C, Araya-Secchi R, Tamilselvan E, Sotomayor M. Structural determinants of protocadherin-15 mechanics and function in hearing and balance perception. Proc Natl Acad Sci U S A. 2020 Sep 22. pii: 1920444117. doi:, 10.1073/pnas.1920444117. PMID:32963095 doi:http://dx.doi.org/10.1073/pnas.1920444117
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