{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T12:42:36Z","timestamp":1791031356353,"version":"4.1.0"},"reference-count":39,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2009,4,13]],"date-time":"2009-04-13T00:00:00Z","timestamp":1239580800000},"content-version":"vor","delay-in-days":2600,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2002,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p><jats:italic>Centruroides sculpturatus<\/jats:italic> Ewing variant 2 toxin (CsE\u2010v2) is a neurotoxin isolated from the venom of a scorpion native to the Arizona desert. The structure of CsE\u2010v2 was solved in two different crystal forms using a combination of molecular replacement and multiple isomorphous replacement techniques. Crystals of CsE\u2010v2 display a temperature\u2010dependent, reversible\u2010phase transition near room temperature. At lower temperature the space group changes from P3<jats:sub>2<\/jats:sub>21 to P3<jats:sub>1<\/jats:sub>21 with an approximate doubling of the <jats:italic>C<\/jats:italic>\u2010axis. The small\u2010cell structure, which has one molecule per asymmetric unit, has an <jats:italic>R<\/jats:italic> factor of 0.229 at 2.8 \u00c5 resolution. The large\u2010cell structure has two molecules per asymmetric unit and was refined at 2.2 \u00c5 resolution to an <jats:italic>R<\/jats:italic> factor of 0.255. CsE\u2010v2 is a rigid, compact structure with four intrachain disulfide bonds. The structure is similar to other long\u2010chain \u03b2 neurotoxins, and the largest differences occur in the last six residues. The high\u2010resolution structure of CsE\u2010v2 corrects an error in the reported C\u2010terminal sequence; the terminal tripeptide sequence is Ser 64\u2010Cys 65\u2010Ser 66 rather than Ser 64\u2010Ser 65\u2010Cys 66. Comparison of CsE\u2010v2 with long\u2010chain \u03b1 toxins reveals four insertions and one deletion, as well as additional residues at the N and C termini. Structural alignment of \u03b1 and \u03b2 toxins suggests that the primary distinguishing feature between the two classes is the length of the loop between the second and third strands in a three\u2010strand \u03b2 sheet. The shorter loop in \u03b1 toxins exposes a critical lysine side chain, whereas the longer loop in \u03b2 toxins buries the corresponding basic residue (either arginine or lysine).<\/jats:p>","DOI":"10.1110\/ps.39202","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T23:59:58Z","timestamp":1027727998000},"page":"479-486","source":"Crossref","is-referenced-by-count":20,"title":["Structure of variant 2 scorpion toxin from <i>Centruroides sculpturatus<\/i> Ewing"],"prefix":"10.1002","volume":"11","author":[{"given":"William J.","family":"Cook","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alan","family":"Zell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dean D.","family":"Watt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven E.","family":"Ealick","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,4,13]]},"reference":[{"key":"e_1_2_7_2_1","first-page":"694","article-title":"Amino acid sequences of neurotoxic protein variants from the venom of Centruroides sculpturatus Ewing","volume":"164","author":"Babin D.R.","year":"1974","journal-title":"Ewing"},{"key":"e_1_2_7_3_1","first-page":"37","article-title":"ALSCRIPT: A tool to format multiple sequence alignments","volume":"6","author":"Barton G. J.","year":"1993","journal-title":"alignments"},{"key":"e_1_2_7_4_1","first-page":"46","article-title":"Extension of molecular replacement: A new search strategy based on Patterson correlation refinement","volume":"46","author":"Br\u00fcnger A.T.","year":"1990","journal-title":"refinement"},{"key":"e_1_2_7_5_1","first-page":"472","article-title":"Free R value: A novel statistical quantity for assessing the accuracy of crystal structures","volume":"355","author":"Br\u00fcnger A.T.","year":"1992","journal-title":"structures"},{"key":"e_1_2_7_6_1","first-page":"458","article-title":"Crystallographic R factor refinement by molecular dynamics","volume":"235","author":"Br\u00fcnger A.T.","year":"1987","journal-title":"dynamics"},{"key":"e_1_2_7_7_1","first-page":"585","article-title":"Slow\u2010cooling protocols for crystallographic refinement by simulated annealing","volume":"46","author":"Br\u00fcnger A.T.","year":"1990","journal-title":"annealing"},{"key":"e_1_2_7_8_1","first-page":"103","article-title":"Ribbon models of macromolecules","volume":"5","author":"Carson M.","year":"1987","journal-title":"macromolecules"},{"key":"e_1_2_7_9_1","first-page":"357","article-title":"Binding of scorpion toxin to receptor sites associated with sodium channels in frog muscle, correlation of voltage\u2010dependent binding with activation","volume":"74","author":"Catterall W.A.","year":"1979","journal-title":"activation"},{"key":"e_1_2_7_10_1","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 suite: Programs for protein crystallography","volume":"50","author":"Collaborative Computational Project, Number 4.","year":"1994","journal-title":"crystallography"},{"key":"e_1_2_7_11_1","first-page":"457","article-title":"Binding of scorpion neurotoxins to chick embryonic heart cells in culture and relationship to calcium uptake and membrane potential","volume":"19","author":"Couraud F.","year":"1980","journal-title":"potential"},{"key":"e_1_2_7_12_1","first-page":"1640","article-title":"Kaliotoxin, a novel peptidyl inhibitor of neuronal BK\u2010type Ca(2+)\u2010activated K+ channels characterized from Androctonus mauretanicus mauretanicus venom","volume":"267","author":"Crest M.","year":"1992","journal-title":"venom"},{"key":"e_1_2_7_13_1","first-page":"12081","article-title":"Preliminary X\u2010ray investigation of CsE\u2010v2 scorpion toxin from Centruroides sculpturatus Ewing: Evidence of a reversible transition between crystal forms","volume":"259","author":"Ealick S.E.","year":"1984","journal-title":"forms"},{"key":"e_1_2_7_14_1","first-page":"392","article-title":"Accurate bond and angle parameters for X\u2010ray protein structure refinement","volume":"47","author":"Engh R.A.","year":"1991","journal-title":"refinement"},{"key":"e_1_2_7_15_1","first-page":"11083","article-title":"Purification and characterization of a unique, potent, peptidyl probe for the high conductance calcium\u2010activated potassium channel from venom of the scorpion Buthus tamulus","volume":"265","author":"Galvez A.","year":"1990","journal-title":"tamulus"},{"key":"e_1_2_7_16_1","first-page":"3329","article-title":"Purification, sequence, and model structure of charybdotoxin, a potent selective inhibitor of calcium\u2010activated potassium channels","volume":"85","author":"Gimenez\u2010Gallego G.","year":"1988","journal-title":"channels"},{"key":"e_1_2_7_17_1","first-page":"125","article-title":"Crystal structures of two \u03b1\u2010like scorpion toxins: Non\u2010proline cis peptide bonds and implications for new binding site selectivity on the sodium channel","volume":"292","author":"He X.\u2010L.","year":"1999","journal-title":"channel"},{"key":"e_1_2_7_18_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444999014614"},{"key":"e_1_2_7_19_1","first-page":"88","article-title":"Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 \u00c5 resolution","volume":"238","author":"Housset D.","year":"1994","journal-title":"resolution"},{"key":"e_1_2_7_20_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0021889887086436"},{"key":"e_1_2_7_21_1","first-page":"449","article-title":"Solution structure of an old world\u2010like neurotoxin from the venom of the new world scorpion Centruroides sculpturatus Ewing","volume":"248","author":"Jablonsky M.J.","year":"1995","journal-title":"Ewing"},{"key":"e_1_2_7_22_1","first-page":"406","article-title":"Solution structure of a beta\u2010neurotoxin from the new world scorpion Centruroides sculpturatus Ewing","volume":"254","author":"Jablonsky M.J.","year":"1999","journal-title":"Ewing"},{"key":"e_1_2_7_23_1","first-page":"100","article-title":"Protein hydration observed by X\u2010ray diffraction; solvation properties of penicillopepsin and neuraminidase crystal structures","volume":"243","author":"Jiang J.\u2010S.","year":"1994","journal-title":"structures"},{"key":"e_1_2_7_24_1","first-page":"1607","article-title":"Two types of scorpion neurotoxins characterized by their binding to two separate receptor sites on rat brain synaptosomes","volume":"95","author":"Jover E.","year":"1980","journal-title":"synaptosomes"},{"key":"e_1_2_7_25_1","first-page":"360","article-title":"Refined solution structure of the anti\u2010mammal and anti\u2010insect LqqIII scorpion toxin: Comparison with other scorpion toxins","volume":"28","author":"Landon C.","year":"1997","journal-title":"toxins"},{"key":"e_1_2_7_26_1","first-page":"2468","article-title":"Proton nuclear magnetic resonance and distance geometry\/simulated annealing studies on the variant\u20101 neurotoxin from the new world scorpion Centruroides sculpturatus Ewing","volume":"33","author":"Lee W.","year":"1994","journal-title":"Ewing"},{"key":"e_1_2_7_27_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1996.0473"},{"key":"e_1_2_7_28_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0365110X52002161"},{"key":"e_1_2_7_29_1","first-page":"491","article-title":"Solvent content of protein crystals","volume":"33","author":"Matthews B.W.","year":"1968","journal-title":"crystals"},{"key":"e_1_2_7_30_1","first-page":"850","article-title":"Effects of scorpion venom on squid axon membranes","volume":"222","author":"Narahashi T.","year":"1972","journal-title":"membranes"},{"key":"e_1_2_7_31_1","first-page":"1095","article-title":"An excitatory scorpion toxin with a distinctive feature: An additional alpha helix at the C terminus and its implications for interaction with insect sodium channels","volume":"6","author":"Oren D.A.","year":"1998","journal-title":"channels"},{"key":"e_1_2_7_32_1","first-page":"80","volume-title":"Isomorphous Replacement and Anomalous Scattering","author":"Otwinoski Z.","year":"1991"},{"key":"e_1_2_7_33_1","first-page":"359","article-title":"Solution structure of toxin 2 from Centruroides noxius Hoffmann, a \u03b2\u2010scorpion neurotoxin acting on sodium channels","volume":"287","author":"Pintar A.","year":"1999","journal-title":"channels"},{"key":"e_1_2_7_34_1","first-page":"175","article-title":"Crystal structure of neurotoxin Ts1 from Tityus serrulatus provides insights into the specificity and toxicity of scorpion toxins","volume":"290","author":"Polikarpov I.","year":"1999","journal-title":"toxins"},{"key":"e_1_2_7_35_1","first-page":"285","article-title":"The primary structure of noxiustoxin: A K+ channel blocker peptide purified from the venom of the scorpion Centruroides noxius Hoffmann","volume":"47","author":"Possani L.D.","year":"1982","journal-title":"Hoffmann"},{"key":"e_1_2_7_36_1","first-page":"140","article-title":"Improved Fourier coefficients for maps using phases from partial structures with errors","volume":"42","author":"Read R.J.","year":"1986","journal-title":"errors"},{"key":"e_1_2_7_37_1","first-page":"115","article-title":"Scorpion neurotoxin: A presynaptic toxin which affects both Na+ and K+ channels in axons","volume":"64","author":"Romey G.","year":"1975","journal-title":"axons"},{"key":"e_1_2_7_38_1","first-page":"244","article-title":"CHAIN\u2014A crystallographic modeling program","volume":"6","author":"Sack J.S.","year":"1988","journal-title":"program"},{"key":"e_1_2_7_39_1","first-page":"2414","article-title":"Solution structures of a highly insecticidal recombinant scorpion alpha\u2010toxin and a mutant with increased activity","volume":"36","author":"Tugarinov V.","year":"1997","journal-title":"activity"},{"key":"e_1_2_7_40_1","first-page":"239","article-title":"Structure of scorpion toxin Variant\u20103 at 1.2 \u00c5 resolution","volume":"227","author":"Zhao B.","year":"1992","journal-title":"resolution"}],"container-title":["Protein Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1110%2Fps.39202","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1110\/ps.39202","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,9]],"date-time":"2023-10-09T17:53:36Z","timestamp":1696874016000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1110\/ps.39202"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,3]]},"references-count":39,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2002,3]]}},"alternative-id":["10.1110\/ps.39202"],"URL":"https:\/\/doi.org\/10.1110\/ps.39202","archive":["Portico"],"relation":{},"ISSN":["0961-8368","1469-896X"],"issn-type":[{"value":"0961-8368","type":"print"},{"value":"1469-896X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2002,3]]}}}