2mhf
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Solution structure of the cyclic-nucleotide binding homology domain of a KCNH channel== |
| + | <StructureSection load='2mhf' size='340' side='right'caption='[[2mhf]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mhf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MHF FirstGlance]. <br> | ||
| + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mhf OCA], [https://pdbe.org/2mhf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mhf RCSB], [https://www.ebi.ac.uk/pdbsum/2mhf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mhf ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A8WHX9_DANRE A8WHX9_DANRE] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The carboxy-terminal region of the KCNH family of potassium channels contains a cyclic-nucleotide binding homology domain (CNBHD) that is important for channel gating and trafficking. The solution structure of the CNBHD of the KCNH potassium of zebrafish was determined using solution NMR spectroscopy. This domain exists as a monomer under solution conditions and adopts a similar fold to that determined by X-ray crystallography. The CNBHD does not bind cAMP because residue Y740 blocks the entry of cyclic-nucleotide to the binding pocket. Relaxation results show that the CNBHD is rigid except that some residues in the loop between beta6 and beta7 are flexible. Our results will be useful to understand the gating mechanism of KCNH family members through the CNBHD. | ||
| - | + | Solution structure of the cyclic-nucleotide binding homology domain of a KCNH channel.,Li Q, Ng HQ, Yoon HS, Kang C J Struct Biol. 2014 Mar 14. pii: S1047-8477(14)00061-6. doi:, 10.1016/j.jsb.2014.03.008. PMID:24632450<ref>PMID:24632450</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2mhf" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Danio rerio]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Li Q]] | ||
| + | [[Category: Ng H]] | ||
Current revision
Solution structure of the cyclic-nucleotide binding homology domain of a KCNH channel
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