dc.creatorKrauchenco, S
dc.creatorPando, SC
dc.creatorMarangoni, S
dc.creatorPolikarpov, I
dc.date2003
dc.dateDEC 26
dc.date2014-11-15T21:27:01Z
dc.date2015-11-26T17:22:02Z
dc.date2014-11-15T21:27:01Z
dc.date2015-11-26T17:22:02Z
dc.date.accessioned2018-03-29T00:09:30Z
dc.date.available2018-03-29T00:09:30Z
dc.identifierBiochemical And Biophysical Research Communications. Academic Press Inc Elsevier Science, v. 312, n. 4, n. 1303, n. 1308, 2003.
dc.identifier0006-291X
dc.identifierWOS:000187252300066
dc.identifier10.1016/j.bbrc.2003.11.062
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/57452
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/57452
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/57452
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1283511
dc.descriptionThe three-dimensional structure of a novel Kunitz (STI) family member, an inhibitor purified from Delonix regia seeds.(DrTI), was solved by molecular replacement method and refined, respectively, to R-factor and R-free values of 21.5% and 25.3% at 1.75 Angstrom resolution. The structure has a classical beta-trefoil fold, however, differently from canonical Kunitz type (STI) inhibitors, its reactive site loop has an insertion of one residue, Glu68, between the residues P1 and P2. Surprisingly, DrTI is an effective inhibitor of trypsin and human plasma kallikrein, but not of chymotrypsin and tissue kallikrein. Putative structural grounds of such specificity are discussed. (C) 2003 Elsevier Inc. All rights reserved.
dc.description312
dc.description4
dc.description1303
dc.description1308
dc.languageen
dc.publisherAcademic Press Inc Elsevier Science
dc.publisherSan Diego
dc.publisherEUA
dc.relationBiochemical And Biophysical Research Communications
dc.relationBiochem. Biophys. Res. Commun.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectKunitz-type inhibitor
dc.subjectKallikrein inhibitor
dc.subjectX-ray structure
dc.subjectbeta-trefoil fold
dc.subjectflamboyant
dc.subjectDelonix regia
dc.subjectFibroblast Growth-factors
dc.subjectTrypsin-inhibitor
dc.subjectProtein Crystallography
dc.subjectChymotrypsin Inhibitor
dc.subjectAngstrom Resolution
dc.subjectSerine-protease
dc.subjectBinding
dc.subjectCrystallization
dc.subjectRefinement
dc.subjectComplex
dc.titleCrystal structure of the Kunitz (STI)-type inhibitor from Delonix regia seeds
dc.typeArtículos de revistas


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