Idioma:

Structural and functional analyses of DM43, a snake venom metalloproteinase inhibitor from Didelphis marsupialis serum

Neves-Ferreira, Ana G C ; Perales, Jonas ; Fox, Jay W ; Shannon, John D ; Makino, Débora L ; Garratt, Richard C ; Domont, Gilberto B

The Journal of biological chemistry, 2002-04, Vol.277 (15), p.13129-13137 [Periódico revisado por pares]

United States

Texto completo disponível

Citações Citado por

Enviar para

Título:
Structural and functional analyses of DM43, a snake venom metalloproteinase inhibitor from Didelphis marsupialis serum
Autor: Neves-Ferreira, Ana G C ; Perales, Jonas ; Fox, Jay W ; Shannon, John D ; Makino, Débora L ; Garratt, Richard C ; Domont, Gilberto B
Assuntos: Amino Acid Sequence ; Animals ; atrolysin ; Blood Proteins - chemistry ; Blood Proteins - isolation & purification ; Blood Proteins - pharmacology ; bothrolysin ; Bothrops ; Crotalid Venoms - enzymology ; Didelphis marsupialis ; DM43 protein ; jararhagin ; Metalloendopeptidases - antagonists & inhibitors ; Models, Molecular ; Molecular Sequence Data ; Opossums ; Protease Inhibitors - chemistry ; Protease Inhibitors - isolation & purification ; Protease Inhibitors - pharmacology ; Protein Structure, Quaternary ; Sequence Homology, Amino Acid ; Serpentes
É parte de: The Journal of biological chemistry, 2002-04, Vol.277 (15), p.13129-13137
Notas: ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
Descrição: 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.
Editor: United States
Idioma: Inglês

Links

View this record in MEDLINE/PubMed

Voltar para lista de resultados

Realização: Logos de Redes Sociais:

Structural and functional analyses of DM43, a snake venom metalloproteinase inhibitor from Didelphis marsupialis serum

Neves-Ferreira, Ana G C ; Perales, Jonas ; Fox, Jay W ; Shannon, John D ; Makino, Débora L ; Garratt, Richard C ; Domont, Gilberto B

United States

Buscando em bases de dados remotas. Favor aguardar.