N. G. Housden

Construction and characterization of protein rLG, a novel 16.5 kDa hybrid protein with a large binding repertoire for immunoglobulin fragments (2005)

Harrison, S.L., Housden, N.G., Gore, M.G.

Several proteins isolated from the surface of Gram-positive pathogenic bacteria have been shown to bind immunoglobulin (Ig) in a non-antigenic manner. The most widely studied of these proteins are...

Different crystal packing in Fab-protein L semi-disordered peptide complex (2005)

Menez, R., Housden, N.G., Harrison, S., Jolivet-Reynaud, C., Gore, M.G., Stura, E.A.

Proteins and peptides with variable degrees of disorder are a challenge for protein crystallization. These may be completely disordered or just contain regions with a high degree of mobility that may...

Comparison of the crystallization and crystal packing of two Fab single-site mutant protein L complexes (2005)

Granata, V., Housden, N.G., Harrison, S., Jolivet-Reynaud, C., Gore, M.G., Stura, E.A.

Protein L from Peptostreptococcus magnus (PpL) is a multidomain protein composed of four or five immunoglobulin-binding domains that target the light chain of a large repertoire of human and murine...

Observation and characterization of the interaction between a single immunoglobulin binding domain of protein L and two equivalents of human kappa light chains (2004)

Housden, N.G., Harrison, S., Housden, H.R., Beckingham, J.A., Roberts, S.A., ...

Detailed stopped-flow studies in combination with site-directed mutagenesis, isothermal titration calorimetry data and x-ray crystallographic knowledge have revealed that the biphasic pre-equilibrium...

Observation and characterization of the interaction between a single immunoglobulin binding domain of protein L and two equivalents of human kappa light chains (2004)

Housden, N.G., Harrison, S., Housden, H.R., Thomas, K.A., Beckingham, J.A., Roberts, S.E., ...

Detailed stopped-flow studies in combination with site-directed mutagenesis, isothermal titration calorimetry data and x-ray crystallographic knowledge have revealed that the biphasic pre-equilibrium...

Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus (2003)

Housden, N.G., Harrison, S., Roberts, S.E., Beckingham, J.A., Graille, M., Stura, E., ...

Protein L is a multidomain cell-wall protein isolated from Peptostreptococcus magnus. It belongs to a group of proteins that contain repeated domains that are able to bind to Igs without stimulating...

Evidence for plasticity and structural mimicry at the immunoglobulin light chain-protein L interface (2002)

Graille, M., Harrison, S., Crump, M.P., Findlow, S.C., Housden, N.G., Muller, B.H., ...

The multidomain bacterial surface protein L (PpL) is a virulence factor expressed by only 10% of Peptostreptococcus magnus strains, and its expression is correlated with bacterial vaginosis. The...

Complex between Peptostreptococcusmagnus ProteinL and a human antibody reveals structural convergence in the interaction modes of fab binding proteins (2001)

Graille, M., Stura, E.A., Housden, N.G., Bottomley, S.P., Beale, D., Taussig, M.J., ...

Background: Peptostreptococcus magnus protein L (PpL) is a multidomain, bacterial surface protein whose presence correlates with virulence. It consists of up to five homologous immunoglobulin binding...

Studies on a single immunoglobulin-binding domain of protein L from Peptostreptococcus magnus: the role of tyrosine-53 in the reaction with human IgG (2001)

Beckingham, J.A., Housden, N.G., Muir, N.M., Bottomley, S.P., Gore, M.G.

Chemical modification experiments with tetranitromethane (TNM) have been used to investigate the role of tyrosine residues in the formation of the complex between PpL (the single Ig-binding domain of...

Studies on a single immunoglobulin-binding domain of protein L from Peptostreptococcus magnus: the role of tyrosine-53 in the reaction with human IgG (2001)

Beckingham, J.A., Housden, N.G., Muir, N.M., Bottomley, S.P., Gore, M.G.

Chemical modification experiments with tetranitromethane (TNM) have been used to investigate the role of tyrosine residues in the formation of the complex between PpL (the single Ig-binding domain of...

Studies on a single immunoglobulin-binding domain of protein L from Peptostreptococcus magnus: the role of tyrosine-53 in the reaction with human IgG.

Beckingham, J A, Housden, N G, Muir, N M, Bottomley, S P, Gore, M G

Chemical modification experiments with tetranitromethane (TNM) have been used to investigate the role of tyrosine residues in the formation of the complex between PpL (the single Ig-binding domain of...

Studies on a single immunoglobulin-binding domain of protein L from Peptostreptococcus magnus: the role of tyrosine-53 in the reaction with human IgG.

Beckingham, J A, Housden, N G, Muir, N M, Bottomley, S P, Gore, M G

Chemical modification experiments with tetranitromethane (TNM) have been used to investigate the role of tyrosine residues in the formation of the complex between PpL (the single Ig-binding domain of...