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| | <StructureSection load='6b25' size='340' side='right'caption='[[6b25]], [[Resolution|resolution]] 2.39Å' scene=''> | | <StructureSection load='6b25' size='340' side='right'caption='[[6b25]], [[Resolution|resolution]] 2.39Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6b25]] 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=6B25 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B25 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6b25]] 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=6B25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B25 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</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]] 2.39Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STAC ([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=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></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=6b25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b25 OCA], [http://pdbe.org/6b25 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b25 RCSB], [http://www.ebi.ac.uk/pdbsum/6b25 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b25 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=6b25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b25 OCA], [https://pdbe.org/6b25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b25 RCSB], [https://www.ebi.ac.uk/pdbsum/6b25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b25 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/STAC_HUMAN STAC_HUMAN]] Probably involved in a neuron-specific signal transduction. | + | [https://www.uniprot.org/uniprot/STAC_HUMAN STAC_HUMAN] Probably involved in a neuron-specific signal transduction. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Excitation-contraction (EC) coupling in skeletal muscle requires functional and mechanical coupling between L-type voltage-gated calcium channels (CaV1.1) and the ryanodine receptor (RyR1). Recently, STAC3 was identified as an essential protein for EC coupling and is part of a group of three proteins that can bind and modulate L-type voltage-gated calcium channels. Here, we report crystal structures of tandem-SH3 domains of different STAC isoforms up to 1.2-A resolution. These form a rigid interaction through a conserved interdomain interface. We identify the linker connecting transmembrane repeats II and III in two different CaV isoforms as a binding site for the SH3 domains and report a crystal structure of the complex with the STAC2 isoform. The interaction site includes the location for a disease variant in STAC3 that has been linked to Native American myopathy (NAM). Introducing the mutation does not cause misfolding of the SH3 domains, but abolishes the interaction. Disruption of the interaction via mutations in the II-III loop perturbs skeletal muscle EC coupling, but preserves the ability of STAC3 to slow down inactivation of CaV1.2.
| + | |
| - | | + | |
| - | Structural insights into binding of STAC proteins to voltage-gated calcium channels.,Wong King Yuen SM, Campiglio M, Tung CC, Flucher BE, Van Petegem F Proc Natl Acad Sci U S A. 2017 Oct 23. pii: 201708852. doi:, 10.1073/pnas.1708852114. PMID:29078335<ref>PMID:29078335</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6b25" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Petegem, F Van]] | + | [[Category: Van Petegem F]] |
| - | [[Category: Yuen, S M.Wong King]] | + | [[Category: Wong King Yuen SM]] |
| - | [[Category: Excitation-contraction coupling]]
| + | |
| - | [[Category: Ion channel adaptor protein]]
| + | |
| - | [[Category: Protein binding]]
| + | |
