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- W2076838529 abstract "Surface proteins on pathogenic strains of Leptospira are involved in host adhesion interactions, an important step in bacterial infection. Lig (Leptospira immunoglobulin (Ig) -like) proteins can bind to human extracellular matrix proteins and have shown promise in typing leptospiral isolates for pathogenesis. Lig proteins are composed of twelve to thirteen Ig-like domain repeats that are anchored to the outer membrane at the N-terminus. Here, we combine experimental data from small-angle x-ray scattering (SAXS) and nuclear magnetic resonance (NMR) to develop a model of the overall architecture of the multi-Ig-like domain chain from LigB. SAXS scattering curves were obtained from constructs containing two to five tandem domains. An ensemble of low resolution envelopes was reconstructed and combined to create a low resolution model of the twelve domains from LigB. In addition, we solved the high resolution NMR structure of the twelfth Ig-like domain from LigB (LigB12). using LigB12-dervied homology models for the other eleven domains, LigB1-11, along with additional experimentally derived NMR constraints, we generated a high resolution model for the Ig-like domain region of LigB. The LigB Ig-like domain architecture should prove useful in understanding the Leptospira surface structure, Lig protein mediated host interactions, and Lig protein accessibility to antibodies." @default.
- W2076838529 created "2016-06-24" @default.
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- W2076838529 date "2013-01-01" @default.
- W2076838529 modified "2023-09-28" @default.
- W2076838529 title "Structural Architecture of the Multi-Immunoglobulin-Like Domain Chain from Ligb" @default.
- W2076838529 doi "https://doi.org/10.1016/j.bpj.2012.11.3151" @default.
- W2076838529 hasPublicationYear "2013" @default.
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