|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Solution structure of a bacterial cyclic nucleotide-activated K+ channel binding domain in the unliganded state== | | ==Solution structure of a bacterial cyclic nucleotide-activated K+ channel binding domain in the unliganded state== |
| - | <StructureSection load='2kxl' size='340' side='right' caption='[[2kxl]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='2kxl' size='340' side='right'caption='[[2kxl]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kxl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700743 Atcc 700743]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KXL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kxl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesorhizobium_loti Mesorhizobium loti]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KXL FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2k0g|2k0g]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mll3241 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=381 ATCC 700743])</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=2kxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxl OCA], [https://pdbe.org/2kxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxl RCSB], [https://www.ebi.ac.uk/pdbsum/2kxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxl 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=2kxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxl OCA], [http://pdbe.org/2kxl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kxl RCSB], [http://www.ebi.ac.uk/pdbsum/2kxl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO]] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</ref> | + | [https://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Cyclic nucleotide-sensitive ion channels, known as HCN and CNG channels, are activated by binding of ligands to a domain (CNBD) located on the cytoplasmic side of the channel. The underlying mechanisms are not well understood. To elucidate the gating mechanism, structures of both the ligand-free and -bound CNBD are required. Several crystal structures of the CNBD from HCN2 and a bacterial CNG channel (MloK1) have been solved. However, for HCN2, the cAMP-free and -bound state did not reveal substantial structural rearrangements. For MloK1, structural information for the cAMP-free state has only been gained from mutant CNBDs. Moreover, in the crystal, the CNBD molecules form an interface between dimers, proposed to be important for allosteric channel gating. Here, we have determined the solution structure by NMR spectroscopy of the cAMP-free wild-type CNBD of MloK1. A comparison of the solution structure of cAMP-free and -bound states reveals large conformational rearrangement on ligand binding. The two structures provide insights on a unique set of conformational events that accompany gating within the ligand-binding site.
| + | |
| - | | + | |
| - | Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel.,Schunke S, Stoldt M, Lecher J, Kaupp UB, Willbold D Proc Natl Acad Sci U S A. 2011 Apr 12;108(15):6121-6. Epub 2011 Mar 23. PMID:21430265<ref>PMID:21430265</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 2kxl" style="background-color:#fffaf0;"></div>
| + | |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ion channels|Ion channels]] | + | *[[Ion channels 3D structures|Ion channels 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 700743]] | + | [[Category: Large Structures]] |
| - | [[Category: Schunke, S]] | + | [[Category: Mesorhizobium loti]] |
| - | [[Category: Stoldt, M]] | + | [[Category: Schunke S]] |
| - | [[Category: Willbold, D]] | + | [[Category: Stoldt M]] |
| - | [[Category: Beta barrel core]] | + | [[Category: Willbold D]] |
| - | [[Category: Helical portion]]
| + | |
| - | [[Category: Ion channel]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Protein phosphate binding cassette in the apo state]]
| + | |
