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| | <StructureSection load='5f3y' size='340' side='right'caption='[[5f3y]], [[Resolution|resolution]] 3.41Å' scene=''> | | <StructureSection load='5f3y' size='340' side='right'caption='[[5f3y]], [[Resolution|resolution]] 3.41Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5f3y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F3Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5F3Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5f3y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F3Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F3Y FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Myo7b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Anks4b, Harp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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]] 3.409Å</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=5f3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f3y OCA], [http://pdbe.org/5f3y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f3y RCSB], [http://www.ebi.ac.uk/pdbsum/5f3y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f3y 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=5f3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f3y OCA], [https://pdbe.org/5f3y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f3y RCSB], [https://www.ebi.ac.uk/pdbsum/5f3y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f3y ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MYO7B_MOUSE MYO7B_MOUSE]] Myosins are actin-based motor molecules with ATPase activity. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. May link the complex to the actin core bundle of microvilli.[UniProtKB:Q6PIF6] [[http://www.uniprot.org/uniprot/ANS4B_MOUSE ANS4B_MOUSE]] As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. Plays a role in assembly of the complex (By similarity). May play a role in cellular response to endoplasmic reticulum stress (PubMed:22589549).[UniProtKB:Q8N8V4]<ref>PMID:22589549</ref> | + | [https://www.uniprot.org/uniprot/MYO7B_MOUSE MYO7B_MOUSE] Myosins are actin-based motor molecules with ATPase activity. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. May link the complex to the actin core bundle of microvilli.[UniProtKB:Q6PIF6] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: He, Y]] | + | [[Category: He Y]] |
| - | [[Category: Li, J]] | + | [[Category: Li J]] |
| - | [[Category: Lu, Q]] | + | [[Category: Lu Q]] |
| - | [[Category: Zhang, M]] | + | [[Category: Zhang M]] |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Motor protein-protein binding complex]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Structural protein]]
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| Structural highlights
Function
MYO7B_MOUSE Myosins are actin-based motor molecules with ATPase activity. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. May link the complex to the actin core bundle of microvilli.[UniProtKB:Q6PIF6]
Publication Abstract from PubMed
Brush border microvilli are actin-based protrusions lining the apical surface of epithelial cells in intestines and proximal tubules of kidneys. While brush border microvilli resemble the relatively well-characterized stereocilia of hair cells, the mechanistic basis of tip-link complex organization in microvilli is poorly understood. Here, we have biochemically and structurally characterized the following pairs of interactions: protocadherin 24 and Harmonin (also known as USH1C or AIE-75), Harmonin and myosin VIIb (MYO7B), Harmonin and ANKS4B, and ANKS4B and MYO7B. We show that Harmonin, ANKS4B, and MYO7B form a stable ternary complex for anchoring microvilli tip-link cadherins. Despite having only Harmonin in common, the microvilli and the stereocilia tip-link complexes are formed via strikingly similar interaction modes. These results not only provide insight into the mechanistic bases of brush border microvilli formation and maintenance but may also be valuable for understanding some gut and/or kidney diseases caused by perturbations of brush border microvilli structures.
Mechanistic Basis of Organization of the Harmonin/USH1C-Mediated Brush Border Microvilli Tip-Link Complex.,Li J, He Y, Lu Q, Zhang M Dev Cell. 2016 Jan 25;36(2):179-89. doi: 10.1016/j.devcel.2015.12.020. PMID:26812017[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li J, He Y, Lu Q, Zhang M. Mechanistic Basis of Organization of the Harmonin/USH1C-Mediated Brush Border Microvilli Tip-Link Complex. Dev Cell. 2016 Jan 25;36(2):179-89. doi: 10.1016/j.devcel.2015.12.020. PMID:26812017 doi:http://dx.doi.org/10.1016/j.devcel.2015.12.020
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