8sib: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 8sib is ON HOLD  until Paper Publication
+==Cryo-EM structure of TRPM7 MHR1-3 domain==
+<StructureSection load='8sib' size='340' side='right'caption='[[8sib]], [[Resolution|resolution]] 2.62&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8sib]] is a 1 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=8SIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SIB FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.62&#8491;</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=8sib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sib OCA], [https://pdbe.org/8sib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sib RCSB], [https://www.ebi.ac.uk/pdbsum/8sib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sib ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRPM7_MOUSE TRPM7_MOUSE] Essential ion channel and serine/threonine-protein kinase. Divalent cation channel permeable to calcium and magnesium. Has a central role in magnesium ion homeostasis and in the regulation of anoxic neuronal cell death. The kinase activity is essential for the channel function. May be involved in a fundamental process that adjusts plasma membrane divalent cation fluxes according to the metabolic state of the cell. Phosphorylates annexin A1 (ANXA1).<ref>PMID:11385574</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The transient receptor potential channel TRPM7 is a master regulator of the organismal balance of divalent cations that plays an essential role in embryonic development, immune responses, cell mobility, proliferation, and differentiation. TRPM7 is implicated in neuronal and cardiovascular disorders, tumor progression and has emerged as a new drug target. Here we use cryo-EM, functional analysis, and molecular dynamics simulations to uncover two distinct structural mechanisms of TRPM7 activation by a gain-of-function mutation and by the agonist naltriben, which show different conformational dynamics and domain involvement. We identify a binding site for highly potent and selective inhibitors and show that they act by stabilizing the TRPM7 closed state. The discovered structural mechanisms provide foundations for understanding the molecular basis of TRPM7 channelopathies and drug development.
-Authors:
+Structural mechanisms of TRPM7 activation and inhibition.,Nadezhdin KD, Correia L, Narangoda C, Patel DS, Neuberger A, Gudermann T, Kurnikova MG, Chubanov V, Sobolevsky AI Nat Commun. 2023 May 8;14(1):2639. doi: 10.1038/s41467-023-38362-3. PMID:37156763<ref>PMID:37156763</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8sib" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Nadezhdin KD]]
+[[Category: Neuberger A]]
+[[Category: Sobolevsky AI]]