6bwi
From Proteopedia
(Difference between revisions)
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==3.7 angstrom cryoEM structure of full length human TRPM4== | ==3.7 angstrom cryoEM structure of full length human TRPM4== | ||
- | <StructureSection load='6bwi' size='340' side='right' caption='[[6bwi]], [[Resolution|resolution]] 3.70Å' scene=''> | + | <StructureSection load='6bwi' size='340' side='right'caption='[[6bwi]], [[Resolution|resolution]] 3.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[6bwi]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BWI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BWI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bwi]] is a 4 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=6BWI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BWI FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRPM4, LTRPC4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bwi OCA], [http://pdbe.org/6bwi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bwi RCSB], [http://www.ebi.ac.uk/pdbsum/6bwi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bwi ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bwi OCA], [http://pdbe.org/6bwi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bwi RCSB], [http://www.ebi.ac.uk/pdbsum/6bwi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bwi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Transient receptor potential melastatin subfamily member 4 (TRPM4) is a widely distributed, calcium-activated, monovalent-selective cation channel. Mutations in human TRPM4 (hTRPM4) result in progressive familial heart block. Here, we report the electron cryomicroscopy structure of hTRPM4 in a closed, Na(+)-bound, apo state at pH 7.5 to an overall resolution of 3.7 A. Five partially hydrated sodium ions are proposed to occupy the center of the conduction pore and the entrance to the coiled-coil domain. We identify an upper gate in the selectivity filter and a lower gate at the entrance to the cytoplasmic coiled-coil domain. Intramolecular interactions exist between the TRP domain and the S4-S5 linker, N-terminal domain, and N and C termini. Finally, we identify aromatic interactions via pi-pi bonds and cation-pi bonds, glycosylation at an N-linked extracellular site, a pore-loop disulfide bond, and 24 lipid binding sites. We compare and contrast this structure with other TRP channels and discuss potential mechanisms of regulation and gating of human full-length TRPM4. | ||
+ | |||
+ | Structure of full-length human TRPM4.,Duan J, Li Z, Li J, Santa-Cruz A, Sanchez-Martinez S, Zhang J, Clapham DE Proc Natl Acad Sci U S A. 2018 Mar 6;115(10):2377-2382. doi:, 10.1073/pnas.1722038115. Epub 2018 Feb 20. PMID:29463718<ref>PMID:29463718</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6bwi" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Human]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Clapham, D E]] | [[Category: Clapham, D E]] | ||
[[Category: Duan, J]] | [[Category: Duan, J]] |
Revision as of 06:37, 3 July 2019
3.7 angstrom cryoEM structure of full length human TRPM4
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Categories: Human | Large Structures | Clapham, D E | Duan, J | Li, J | Li, Z | Zhang, J | Cryoem | Human full length trpm7 | Membrane protein