Solution Structure of Kurtoxin: A Gating Modifier Selective for Cav3 Voltage-Gated Ca2+ Channels
DC Field | Value | Language |
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dc.contributor.author | Lee, Chul Won | - |
dc.contributor.author | Bae, Chanhyung | - |
dc.contributor.author | Lee, Jaeho | - |
dc.contributor.author | Ryu, Jae Ha | - |
dc.contributor.author | Kim, Ha Hyung | - |
dc.contributor.author | Kohno, Toshiyuki | - |
dc.contributor.author | Swartz, Kenton J. | - |
dc.contributor.author | Kim, Jae Il | - |
dc.date.available | 2019-05-29T07:39:04Z | - |
dc.date.issued | 2012-03 | - |
dc.identifier.issn | 0006-2960 | - |
dc.identifier.issn | 1520-4995 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/20445 | - |
dc.description.abstract | Kurtoxin is a 63-amino acid polypeptide isolated from the venom of the South African scorpion Parabuthus transvaalicus. It is the first and only peptide ligand known to interact with Cav3 (T-type) voltage-gated Ca2+ channels with high affinity and to modify the voltage-dependent gating of these channels. Here we describe the nuclear magnetic resonance (NMR) solution structure of kurtoxin determined using two- and three-dimensional NMR spectroscopy with dynamical simulated annealing calculations. The molecular structure of the toxin was highly similar to those of scorpion alpha-toxins and contained an alpha-helix, three beta-strands, and several turns stabilized by four disulfide bonds. This so-called "cysteine-stabilized alpha-helix and beta-sheet (CS alpha beta)" motif is found in a number of functionally varied small proteins. A detailed comparison of the backbone structure of kurtoxin with those of the scorpion a-toxins revealed that three regions [first long loop (Asp(8)-Ile(15)), beta-hairpin loop (Gly(39)-Leu(42)), and C-terminal segment (Arg(57)-Ala(63))] in kurtoxin significantly differ from the corresponding regions in scorpion alpha-toxins, suggesting that these regions may be important for interacting with Cav3 (T-type) Ca2+ channels. In addition, the surface profile of kurtoxin shows a larger and more focused electropositive patch along with a larger hydrophobic surface compared to those seen on scorpion alpha-toxins. These distinct surface properties of kurtoxin could explain its binding to Cav3 (T-type) voltage-gated Ca2+ channels. | - |
dc.format.extent | 12 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.title | Solution Structure of Kurtoxin: A Gating Modifier Selective for Cav3 Voltage-Gated Ca2+ Channels | - |
dc.type | Article | - |
dc.identifier.doi | 10.1021/bi201633j | - |
dc.identifier.bibliographicCitation | BIOCHEMISTRY, v.51, no.9, pp 1862 - 1873 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000301021100006 | - |
dc.identifier.scopusid | 2-s2.0-84863288252 | - |
dc.citation.endPage | 1873 | - |
dc.citation.number | 9 | - |
dc.citation.startPage | 1862 | - |
dc.citation.title | BIOCHEMISTRY | - |
dc.citation.volume | 51 | - |
dc.type.docType | Article | - |
dc.publisher.location | 미국 | - |
dc.subject.keywordPlus | DEPENDENT K+ CHANNEL | - |
dc.subject.keywordPlus | ALPHA-LIKE TOXIN | - |
dc.subject.keywordPlus | NUCLEAR-MAGNETIC-RESONANCE | - |
dc.subject.keywordPlus | POTATO CARBOXYPEPTIDASE INHIBITOR | - |
dc.subject.keywordPlus | 3-DIMENSIONAL SOLUTION STRUCTURE | - |
dc.subject.keywordPlus | ANDROCTONUS-AUSTRALIS HECTOR | - |
dc.subject.keywordPlus | RELAXATION MATRIX ANALYSIS | - |
dc.subject.keywordPlus | BUTHUS-MARTENSII KARSCH | - |
dc.subject.keywordPlus | OMEGA-GRAMMOTOXIN-SIA | - |
dc.subject.keywordPlus | CALCIUM-CHANNELS | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | sci | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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