Author | Ferreira, Ana G. C. Neves | |
Author | Perales, Jonas | |
Author | Fox, Jay W. | |
Author | Shannon, John D. | |
Author | Makino, Débora L. | |
Author | Garratt, Richard C. | |
Author | Domont, Gilberto B. | |
Access date | 2020-05-01T18:49:39Z | |
Available date | 2020-05-01T18:49:39Z | |
Document date | 2002 | |
Citation | FERREIRA, Ana G. C. Neves et al. Structural and Functional Analyses of DM43, a Snake Venom Metalloproteinase Inhibitor from Didelphis marsupialis Serum. The Journal of Biological Chemistry, v. 277, n. 15, p. 13129-13137, 2002. | pt_BR |
ISSN | 0021-9258 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/41062 | |
Description | Publisher's version/PDF may be used after a 12 months embargo period. Acesso aberto em 01/04/2020 - https://www.jbc.org/content/277/15/13129.full.pdf | pt_BR |
Language | eng | pt_BR |
Publisher | American Society for Biochemistry and Molecular Biology | pt_BR |
Rights | open access | pt_BR |
Subject in Portuguese | Análises Estruturais e Funcionais | pt_BR |
Subject in Portuguese | DM43 | pt_BR |
Subject in Portuguese | Veneno de Cobra | pt_BR |
Subject in Portuguese | Inibidor de metaloproteinase | pt_BR |
Subject in Portuguese | Soro de Didelphis marsupialis | pt_BR |
Title | Structural and functional analyses of DM43, a snake venom metalloproteinase inhibitor from Didelphis marsupialis serum | pt_BR |
Type | Article | pt_BR |
DOI | 10.1074/jbc.M200589200 | |
Abstract | DM43, an opossum serum protein inhibitor of snake venom metalloproteinases, has been completely sequenced, and its disulfide bond pattern has been experimentally determined. It shows homology to human alpha(1)B-glycoprotein, a plasma protein of unknown function and a member of the immunoglobulin supergene family. Size exclusion and dynamic laser light scattering data indicated that two monomers of DM43, each composed of three immunoglobulin-like domains, associated to form a homodimer in solution. Analysis of its glycan moiety showed the presence of N-acetylglucosamine, mannose, galactose, and sialic acid, most probably forming four biantennary N-linked chains. DM43 inhibited the fibrinogenolytic activities of bothrolysin and jararhagin and formed 1:1 stoichiometric stable complexes with both metalloproteinases. DM43 was ineffective against atrolysin C or A. No complex formation was detected between DM43 and jararhagin C, indicating the essential role of the metalloproteinase domain for interaction. Homology modeling based on the crystal structure of a killer cell inhibitory receptor suggested the existence of an I-type Ig fold, a hydrophobic dimerization surface and six surface loops potentially forming the metalloproteinase-binding surface on DM43. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Fisiologia e Farmacodinâmica. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Fisiologia e Farmacodinâmica. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | University of Virginia. Department of Microbiology. Charlottesville, Virginia, USA. | pt_BR |
Affilliation | University of Virginia. Department of Microbiology. Charlottesville, Virginia, USA. | pt_BR |
Affilliation | Universidade de São Paulo. Instituto de Física de Sâo Carlos. Departamento de Física e Informática. São Carlos, SP, Brasil. | pt_BR |
Affilliation | Universidade de São Paulo. Instituto de Física de Sâo Carlos. Departamento de Física e Informática. São Carlos, SP, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Química. Departamento de Bioquímica. Rio de Janeiro, RJ, Brasil. | pt_BR |
Subject | Structural and Functional Analyses | pt_BR |
Subject | DM43 | pt_BR |
Subject | Snake Venom | pt_BR |
Subject | Metalloproteinase Inhibitor | pt_BR |
Subject | Didelphis marsupialis Serum | pt_BR |
e-ISSN | 1083-351X | |