Matches in SemOpenAlex for { <https://semopenalex.org/work/W2078091344> ?p ?o ?g. }
Showing items 1 to 73 of
73
with 100 items per page.
- W2078091344 endingPage "11006" @default.
- W2078091344 startingPage "10998" @default.
- W2078091344 abstract "Noxiustoxin (NxTX) and iberiotoxin (IbTX) exhibit extraordinary differences in their ability to inhibit current through the large-conductance calcium-activated potassium (maxi-K) and voltage-gated potassium (Kv1.3) channels. The three-dimensional structures of NxTX and IbTX display differences in their α/β turn and in the length of the α-carbon backbone. To understand the role of these differences in defining specificity, we constructed two NxTX mutants, NxTX−IbTX I and NxTX−IbTX II, and solved their solution structures by 1H NMR spectroscopy. For NxTX−IbTX I, seven amino acids comprising the α/β turn in NxTX are replaced with six amino acids from the corresponding α/β turn in IbTX (NxTX-YGSSAGA21-27FGVDRF21-26). In addition, NxTX−IbTX II contained the S14W mutation and deletion of the N- and C-terminal residues. Both NxTX−IbTX I and NxTX−IbTX II exhibit an α/β scaffold structure typical of the α-K channel toxins. A helix is present from residues 10 to 19 in NxTX−IbTX I and from residues 13 to 19 in NxTX−IbTX II. The β-sheet, defined by three antiparallel strands, is one residue longer in NxTX−IbTX I relative to NxTX−IbTX II. The two toxins also differ in the structure of the α/β turn with NxTX−IbTX I resembling that of IbTX and with NxTX−IbTX II resembling that of NxTX. These differences in the β-sheet and α/β turn alter the dimensions of the toxin−channel interaction surface and provide insight into how these NxTX mutations alter K+ channel specificity for the maxi-K and Kv1.3 channels." @default.
- W2078091344 created "2016-06-24" @default.
- W2078091344 creator A5015370358 @default.
- W2078091344 creator A5017924237 @default.
- W2078091344 creator A5029831246 @default.
- W2078091344 creator A5031345616 @default.
- W2078091344 creator A5073329018 @default.
- W2078091344 creator A5077763814 @default.
- W2078091344 date "2001-08-24" @default.
- W2078091344 modified "2023-09-26" @default.
- W2078091344 title "Structural Basis for α-K Toxin Specificity for K<sup>+</sup> Channels Revealed through the Solution <sup>1</sup>H NMR Structures of Two Noxiustoxin−Iberiotoxin Chimeras" @default.
- W2078091344 cites W1555733423 @default.
- W2078091344 cites W1969239953 @default.
- W2078091344 cites W1972459558 @default.
- W2078091344 cites W1975459052 @default.
- W2078091344 cites W1988915035 @default.
- W2078091344 cites W1992496710 @default.
- W2078091344 cites W1997624484 @default.
- W2078091344 cites W2002195659 @default.
- W2078091344 cites W2003802570 @default.
- W2078091344 cites W2039975948 @default.
- W2078091344 cites W2074770586 @default.
- W2078091344 cites W2131573781 @default.
- W2078091344 cites W2143070723 @default.
- W2078091344 cites W2154049339 @default.
- W2078091344 cites W2949250147 @default.
- W2078091344 doi "https://doi.org/10.1021/bi010228e" @default.
- W2078091344 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11551195" @default.
- W2078091344 hasPublicationYear "2001" @default.
- W2078091344 type Work @default.
- W2078091344 sameAs 2078091344 @default.
- W2078091344 citedByCount "19" @default.
- W2078091344 countsByYear W20780913442012 @default.
- W2078091344 countsByYear W20780913442014 @default.
- W2078091344 countsByYear W20780913442015 @default.
- W2078091344 countsByYear W20780913442016 @default.
- W2078091344 crossrefType "journal-article" @default.
- W2078091344 hasAuthorship W2078091344A5015370358 @default.
- W2078091344 hasAuthorship W2078091344A5017924237 @default.
- W2078091344 hasAuthorship W2078091344A5029831246 @default.
- W2078091344 hasAuthorship W2078091344A5031345616 @default.
- W2078091344 hasAuthorship W2078091344A5073329018 @default.
- W2078091344 hasAuthorship W2078091344A5077763814 @default.
- W2078091344 hasConcept C12554922 @default.
- W2078091344 hasConcept C2779411790 @default.
- W2078091344 hasConcept C83743174 @default.
- W2078091344 hasConcept C86803240 @default.
- W2078091344 hasConceptScore W2078091344C12554922 @default.
- W2078091344 hasConceptScore W2078091344C2779411790 @default.
- W2078091344 hasConceptScore W2078091344C83743174 @default.
- W2078091344 hasConceptScore W2078091344C86803240 @default.
- W2078091344 hasIssue "37" @default.
- W2078091344 hasLocation W20780913441 @default.
- W2078091344 hasLocation W20780913442 @default.
- W2078091344 hasOpenAccess W2078091344 @default.
- W2078091344 hasPrimaryLocation W20780913441 @default.
- W2078091344 hasRelatedWork W1968129587 @default.
- W2078091344 hasRelatedWork W2072549712 @default.
- W2078091344 hasRelatedWork W2079511260 @default.
- W2078091344 hasRelatedWork W2126385830 @default.
- W2078091344 hasRelatedWork W2312672762 @default.
- W2078091344 hasRelatedWork W2381554007 @default.
- W2078091344 hasRelatedWork W2418008882 @default.
- W2078091344 hasRelatedWork W2418695996 @default.
- W2078091344 hasRelatedWork W2756445047 @default.
- W2078091344 hasRelatedWork W3029613312 @default.
- W2078091344 hasVolume "40" @default.
- W2078091344 isParatext "false" @default.
- W2078091344 isRetracted "false" @default.
- W2078091344 magId "2078091344" @default.
- W2078091344 workType "article" @default.