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Three-Dimensional Modelling of Honeybee Venom Allergenic Proteases: Relation to Allergenicity

dc.contributor.authorGeorgieva, Dessislava
dc.contributor.authorGreunke, Kerstin
dc.contributor.authorArni, Raghuvir K. [UNESP]
dc.contributor.authorBetzel, Christian
dc.contributor.institutionUniv Hamburg
dc.contributor.institutionProt Ligand Struct PLS Design GmbH
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T14:02:39Z
dc.date.available2014-05-20T14:02:39Z
dc.date.issued2011-05-01
dc.description.abstractApi SI and Api SIT are serine proteases of the honeybee venom containing allergenic determinants. Each protease consists of two structural modules: an N-terminal CUB (Api SI) or a clip domain (Api SII) and a C-terminal serine protease-like (SPL) domain. Both domains are connected with a linker peptide. The knowledge about the structure and function of Api SI and Api SII is limited mainly to their amino acid sequences. We constructed 3-D models of the two proteases using their amino acid sequences and crystallographic coordinates of related proteins. The models of the SPL domains were built using the structure of the prophenoloxidase-activating factor (PPAF)-II as a template. For modelling of the Api SI CUB domain the coordinates of porcine spermadhesin PSP-I were used. The models revealed the catalytic and substrate-binding sites and the negatively charged residue responsible for the trypsin-like activity. IgE-binding and antigenic sites in the two allergens were predicted using the models and programs based on the structure of known epitopes. Api SI and Api SII show structural and functional similarity to the members of the PPAF-II family. Most probably, they are part of the defence system of Apis mellifera.en
dc.description.affiliationUniv Hamburg, Inst Biochem & Mol Biol, Lab Struct Biol Infect & Inflammat, DESY, D-22603 Hamburg, Germany
dc.description.affiliationProt Ligand Struct PLS Design GmbH, Hamburg, Germany
dc.description.affiliationIBILCE UNESP, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespIBILCE UNESP, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.sponsorshipDeutsche Forschungsgemeinschaft (DFG)
dc.description.sponsorshipRIS Project
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIdDFG: BE 1443-18-1
dc.format.extent305-312
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/21812349
dc.identifier.citationZeitschrift Fur Naturforschung Section C-a Journal of Biosciences. Tubingen: Verlag Z Naturforsch, v. 66, n. 5-6, p. 305-312, 2011.
dc.identifier.issn0939-5075
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.scopus2-s2.0-79959626480
dc.identifier.urihttp://hdl.handle.net/11449/22086
dc.identifier.wosWOS:000293804800015
dc.language.isoeng
dc.publisherVerlag Z Naturforsch
dc.relation.ispartofZeitschrift fur Naturforschung - Section C Journal of Biosciences
dc.relation.ispartofjcr0.882
dc.relation.ispartofsjr0,288
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectHoneybee Venomen
dc.subjectAllergenic Proteasesen
dc.subjectProtein Modellingen
dc.titleThree-Dimensional Modelling of Honeybee Venom Allergenic Proteases: Relation to Allergenicityen
dc.typeArtigo
dcterms.rightsHolderVerlag Z Naturforsch
unesp.author.lattes9162508978945887[3]
unesp.author.orcid0000-0003-2460-1145[3]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Letras e Ciências Exatas, São José do Rio Pretopt
unesp.departmentFísica - IBILCEpt

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