7n4p: Difference between revisions
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The | ==Crystal Structure of Lizard Cadherin-23 EC1-2== | ||
<StructureSection load='7n4p' size='340' side='right'caption='[[7n4p]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7n4p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anolis_carolinensis Anolis carolinensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N4P 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]] 2.097Å</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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7n4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n4p OCA], [https://pdbe.org/7n4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n4p RCSB], [https://www.ebi.ac.uk/pdbsum/7n4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n4p ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/R4GAX0_ANOCA R4GAX0_ANOCA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The sensory epithelium of the inner ear, found in all extant lineages of vertebrates, has been subjected to over 500 million years of evolution, resulting in the complex inner ear of modern vertebrates. Inner-ear adaptations are as diverse as the species in which they are found, and such unique anatomical variations have been well studied. However, the evolutionary details of the molecular machinery that is required for hearing are less well known. Two molecules that are essential for hearing in vertebrates are cadherin-23 and protocadherin-15, proteins whose interaction with one another acts as the focal point of force transmission when converting sound waves into electrical signals that the brain can interpret. This interaction exists in every lineage of vertebrates, but little is known about the structure or mechanical properties of these proteins in most non-mammalian lineages. Here, we use various techniques to characterize the evolution of this protein interaction. Results show how evolutionary sequence changes in this complex affect its biophysical properties both in simulations and experiments, with variations in interaction strength and dynamics among extant vertebrate lineages. Evolutionary simulations also characterize how the biophysical properties of the complex in turn constrain its evolution and provide a possible explanation for the increase in deafness-causing mutants observed in cadherin-23 relative to protocadherin-15. Together, these results suggest a general picture of tip-link evolution in which selection acted to modify the tip-link interface, while subsequent neutral evolution combined with varying degrees of purifying selection drove additional diversification in modern tetrapods. | |||
Interpreting the Evolutionary Echoes of a Protein Complex Essential for Inner-Ear Mechanosensation.,Nisler CR, Narui Y, Scheib E, Choudhary D, Bowman JD, Mandayam Bharathi H, Lynch VJ, Sotomayor M Mol Biol Evol. 2023 Mar 13:msad057. doi: 10.1093/molbev/msad057. PMID:36911992<ref>PMID:36911992</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7n4p" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cadherin 3D structures|Cadherin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Anolis carolinensis]] | |||
[[Category: Large Structures]] | |||
[[Category: Nisler CR]] | |||
[[Category: Sotomayor M]] | |||
Latest revision as of 12:22, 25 October 2023
Crystal Structure of Lizard Cadherin-23 EC1-2Crystal Structure of Lizard Cadherin-23 EC1-2
Structural highlights
FunctionPublication Abstract from PubMedThe sensory epithelium of the inner ear, found in all extant lineages of vertebrates, has been subjected to over 500 million years of evolution, resulting in the complex inner ear of modern vertebrates. Inner-ear adaptations are as diverse as the species in which they are found, and such unique anatomical variations have been well studied. However, the evolutionary details of the molecular machinery that is required for hearing are less well known. Two molecules that are essential for hearing in vertebrates are cadherin-23 and protocadherin-15, proteins whose interaction with one another acts as the focal point of force transmission when converting sound waves into electrical signals that the brain can interpret. This interaction exists in every lineage of vertebrates, but little is known about the structure or mechanical properties of these proteins in most non-mammalian lineages. Here, we use various techniques to characterize the evolution of this protein interaction. Results show how evolutionary sequence changes in this complex affect its biophysical properties both in simulations and experiments, with variations in interaction strength and dynamics among extant vertebrate lineages. Evolutionary simulations also characterize how the biophysical properties of the complex in turn constrain its evolution and provide a possible explanation for the increase in deafness-causing mutants observed in cadherin-23 relative to protocadherin-15. Together, these results suggest a general picture of tip-link evolution in which selection acted to modify the tip-link interface, while subsequent neutral evolution combined with varying degrees of purifying selection drove additional diversification in modern tetrapods. Interpreting the Evolutionary Echoes of a Protein Complex Essential for Inner-Ear Mechanosensation.,Nisler CR, Narui Y, Scheib E, Choudhary D, Bowman JD, Mandayam Bharathi H, Lynch VJ, Sotomayor M Mol Biol Evol. 2023 Mar 13:msad057. doi: 10.1093/molbev/msad057. PMID:36911992[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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