{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T20:47:17Z","timestamp":1790628437966,"version":"4.1.0"},"reference-count":54,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2009,1,1]],"date-time":"2009-01-01T00:00:00Z","timestamp":1230768000000},"content-version":"vor","delay-in-days":1919,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2003,10]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    BaP1 is a 22.7\u2010kD P\u2010I\u2010type zinc\u2010dependent metalloproteinase isolated from the venom of the snake\n                    <jats:italic>Bothrops asper<\/jats:italic>\n                    , a medically relevant species in Central America. This enzyme exerts multiple tissue\u2010damaging activities, including hemorrhage, myonecrosis, dermonecrosis, blistering, and edema. BaP1 is a single chain of 202 amino acids that shows highest sequence identity with metalloproteinases isolated from the venoms of snakes of the subfamily Crotalinae. It has six Cys residues involved in three disulfide bridges (Cys 117\u2013Cys 197, Cys 159\u2013Cys 181, Cys 157\u2013Cys 164). It has the consensus sequence H\n                    <jats:sub>142<\/jats:sub>\n                    E\n                    <jats:sub>143<\/jats:sub>\n                    XXH\n                    <jats:sub>146<\/jats:sub>\n                    XXGXXH\n                    <jats:sub>152<\/jats:sub>\n                    , as well as the sequence C\n                    <jats:sub>164<\/jats:sub>\n                    I\n                    <jats:sub>165<\/jats:sub>\n                    M\n                    <jats:sub>166<\/jats:sub>\n                    , which characterize the \u201cmetzincin\u201d superfamily of metalloproteinases. The active\u2010site cleft separates a major subdomain (residues 1\u2013152), comprising four \u03b1\u2010helices and a five\u2010stranded \u03b2\u2010sheet, from the minor subdomain, which is formed by a single \u03b1\u2010helix and several loops. The catalytic zinc ion is coordinated by the N\n                    <jats:sub>\u03b52<\/jats:sub>\n                    nitrogen atoms of His 142, His 146, and His 152, in addition to a solvent water molecule, which in turn is bound to Glu 143. Several conserved residues contribute to the formation of the hydrophobic pocket, and Met 166 serves as a hydrophobic base for the active\u2010site groups. Sequence and structural comparisons of hemorrhagic and nonhemorrhagic P\u2010I metalloproteinases from snake venoms revealed differences in several regions. In particular, the loop comprising residues 153 to 176 has marked structural differences between metalloproteinases with very different hemorrhagic activities. Because this region lies in close proximity to the active\u2010site microenvironment, it may influence the interaction of these enzymes with physiologically relevant substrates in the extracellular matrix.\n                  <\/jats:p>","DOI":"10.1110\/ps.03102403","type":"journal-article","created":{"date-parts":[[2003,9,19]],"date-time":"2003-09-19T15:33:49Z","timestamp":1063985629000},"page":"2273-2281","source":"Crossref","is-referenced-by-count":117,"title":["Amino acid sequence and crystal structure of BaP1, a metalloproteinase from\n                    <i>Bothrops asper<\/i>\n                    snake venom that exerts multiple tissue\u2010damaging activities"],"prefix":"10.1002","volume":"12","author":[{"given":"Leandra","family":"Watanabe","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John D.","family":"Shannon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard H.","family":"Valente","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexandra","family":"Rucavado","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alberto","family":"Alape\u2010Gir\u00f3n","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aura S.","family":"Kamiguti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R. David G.","family":"Theakston","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jay W.","family":"Fox","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos\u00e9 Mar\u00eda","family":"Guti\u00e9rrez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Raghuvir K.","family":"Arni","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,1]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0934-8832(11)80175-7"},{"key":"e_1_2_6_3_1","first-page":"763","article-title":"Proteolytic digestion of non\u2010collagenous basement membrane proteins by the hemorrhagic metalloproteinase HT\u2010e from Crotalus atrox venom","volume":"50","author":"Baramova E.N.","year":"1991","journal-title":"Biomed. Biochim. Acta"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/0163-7258(94)90049-3"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(95)48023-4"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(93)80312-I"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1208\/ps030216"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.93.7.2749"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444998003254"},{"key":"e_1_2_6_10_1","unstructured":"2002 Delano Scientific San Carlos CA W.S. Delano The PyMOL molecular graphics system"},{"key":"e_1_2_6_11_1","first-page":"667","volume-title":"Clinical toxicology of animal venoms and poisons","author":"Fan H.W.","year":"1995"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1080\/09629350020025728"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0167-4838(00)00128-X"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1993.tb06099.x"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1994.1392"},{"key":"e_1_2_6_16_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1998.2110"},{"key":"e_1_2_6_17_1","first-page":"645","volume-title":"Clinical toxicology of animal venoms and poisons","author":"Guti\u00e9rrez J.M.","year":"1995"},{"key":"e_1_2_6_18_1","doi-asserted-by":"publisher","DOI":"10.1016\/0041-0101(95)00085-Z"},{"key":"e_1_2_6_19_1","first-page":"1295","volume-title":"Handbook of proteolytic enzymes","author":"Guti\u00e9rrez J.M.","year":"1998"},{"key":"e_1_2_6_20_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0300-9084(00)01163-9"},{"key":"e_1_2_6_21_1","doi-asserted-by":"publisher","DOI":"10.1016\/0041-0101(94)00138-X"},{"key":"e_1_2_6_22_1","doi-asserted-by":"publisher","DOI":"10.1080\/10408449991349168"},{"key":"e_1_2_6_23_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(96)66024-8"},{"key":"e_1_2_6_24_1","doi-asserted-by":"publisher","DOI":"10.1006\/abbi.1994.1026"},{"key":"e_1_2_6_25_1","doi-asserted-by":"publisher","DOI":"10.1107\/S090744490200656X"},{"key":"e_1_2_6_26_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1432-1327.1999.00525.x"},{"key":"e_1_2_6_27_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.272.20.13094"},{"key":"e_1_2_6_28_1","doi-asserted-by":"publisher","DOI":"10.1006\/abbi.1999.1517"},{"key":"e_1_2_6_29_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0108767390010224"},{"key":"e_1_2_6_30_1","doi-asserted-by":"publisher","DOI":"10.1016\/0041-0101(96)00017-7"},{"key":"e_1_2_6_31_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj3200635"},{"key":"e_1_2_6_32_1","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.jbchem.a021215"},{"key":"e_1_2_6_33_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0021889892009944"},{"key":"e_1_2_6_34_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00193a006"},{"key":"e_1_2_6_35_1","doi-asserted-by":"publisher","DOI":"10.1021\/ar00153a003"},{"key":"e_1_2_6_36_1","doi-asserted-by":"publisher","DOI":"10.1006\/abbi.1999.1372"},{"key":"e_1_2_6_37_1","first-page":"760","article-title":"Collaborative Computational Project, Number 4. The CCP4 Suite: Programs for protein crystallogaphy","volume":"50","author":"Navaza J.","year":"1994","journal-title":"Acta Crystallogr. A"},{"key":"e_1_2_6_38_1","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-642-66913-2_14"},{"key":"e_1_2_6_39_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(97)76066-X"},{"key":"e_1_2_6_40_1","doi-asserted-by":"publisher","DOI":"10.1385\/MB:22:1:051"},{"key":"e_1_2_6_41_1","first-page":"601","volume-title":"Handbook of toxinology","author":"Ownby C.L.","year":"1990"},{"key":"e_1_2_6_42_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.85.8.2444"},{"key":"e_1_2_6_43_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0168-9002(97)01202-3"},{"key":"e_1_2_6_44_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0909049597014684"},{"key":"e_1_2_6_45_1","doi-asserted-by":"publisher","DOI":"10.1006\/exmp.1995.1042"},{"key":"e_1_2_6_46_1","first-page":"245","article-title":"Blister formation and skin damage induced by BaP1, a haemorhagic metalloproteinase from the venom of the snake Bothrops asper","volume":"79","author":"Rucavado A.","year":"1998","journal-title":"Int. J. Exp. Pathol."},{"key":"e_1_2_6_47_1","doi-asserted-by":"publisher","DOI":"10.1080\/09629350220131980"},{"key":"e_1_2_6_48_1","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560040502"},{"key":"e_1_2_6_49_1","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.jbchem.a122805"},{"key":"e_1_2_6_50_1","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.jbchem.a123270"},{"key":"e_1_2_6_51_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1432-1327.2000.01129.x"},{"key":"e_1_2_6_52_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444902003633"},{"key":"e_1_2_6_53_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.18.8447"},{"key":"e_1_2_6_54_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj3070411"},{"key":"e_1_2_6_55_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444999010306"}],"container-title":["Protein Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1110%2Fps.03102403","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1110\/ps.03102403","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,9]],"date-time":"2023-10-09T16:10:18Z","timestamp":1696867818000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1110\/ps.03102403"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,10]]},"references-count":54,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2003,10]]}},"alternative-id":["10.1110\/ps.03102403"],"URL":"https:\/\/doi.org\/10.1110\/ps.03102403","archive":["Portico"],"relation":{},"ISSN":["0961-8368","1469-896X"],"issn-type":[{"value":"0961-8368","type":"print"},{"value":"1469-896X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2003,10]]}}}