2ao1

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

A THEORETICAL MODEL FOR THE STRUCTURE OF BRSV G PROTEIN IMMUNODOMINANT REGION IN A BRAZILIAN MUTANT ISOLATEA THEORETICAL MODEL FOR THE STRUCTURE OF BRSV G PROTEIN IMMUNODOMINANT REGION IN A BRAZILIAN MUTANT ISOLATE

Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed Bovine respiratory syncytial virus (BRSV) causes lower respiratory tract disease in young cattle. Recently, it was possible to determine the sequence of the G protein gene, which plays a role in the attachment of BRSV particles to the cells, from three distinct Brazilian isolates. The phylogenetic analysis conducted here using those sequences compared to other worldwide distributed isolates of BRSV allow us to allocate Brazilian strains within the subgroup B, which was no longer found in the world since the 1970s. One of the Brazilian strains has a major mutation between amino acid residues 173 and 178, within the central hydrophobic conserved region, exactly on the site of two of the four cysteine-noose forming cysteine residues. Homology modeling with the previously determined NMR structure of this protein domain was made to check whether these mutations altered the three-dimensional conformation of this immunodominant region. Possible consequences on the biological effects induced by such mutation on the G protein are discussed. Phylogenetic relationships of Brazilian bovine respiratory syncytial virus isolates and molecular homology modeling of attachment glycoprotein.,Spilki FR, Almeida RS, Domingues HG, D'Arce RC, Ferreira HL, Campalans J, Costa SC, Arns CW Virus Res. 2006 Mar;116(1-2):30-7. Epub 2006 Jan 4. PMID:16387381 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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