Backbone Dynamics of a Domain of Protein L Which Binds to Immunoglobulin Light Chains

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Abstract
Protein L is a multidomain protein expressed at the surface of some strains of the anaerobic bacterial species Peptostreptococcus magnus. The molecule interacts with the variable domain of immunoglobulin (Ig) light chains through five repeated homologous domains denoted B1 to B5. The fold of the Ig-light-chain-binding B1 domain of protein L (PLB1) has been shown to comprise an α-helix packed against a four-stranded β-sheet and therefore resembles the structure of the IgG-binding domains of streptococcal protein G. In the present study, amide-proton exchange and 15N-relaxation NMR measurements were performed on the B1 domain to investigate its backbone mobility. It was shown that the folded portion of PLB1 is rigid with no regions of significantly higher flexibility than average. The N-terminus, however, is highly flexible consistent with earlier studies on the solution structure of PLB1. Comparison of the amide-proton-exchange data with similar measurements performed on the IgG-binding domains of protein G indicates that the two proteins have different exchange behaviors in heir second β-strands. Both protein G and L employ this region of their structures for binding to immunoglobulins since the interaction of protein G and protein L with IgG Fab and the Ig light chain, respectively, involves residues from the second β-strand.