Abstract
The agglutinin-like-sequence (ALS) family of adhesion proteins are a key virulence factor for C. albicans. These proteins have been implicated in several functions, notably adhesion and invasion of different cell types, as well as binding to peptides and proteins in the cell surface and extracellular matrix. In order to understand their binding mechanism and en route to a full structural determination by NMR, here we report the resonance assignments of backbone atoms plus Ile, Leu and Val methyls for residues 18–329 of ALS1, which comprises the 33.5 kDa binding domain.
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Acknowledgments
This work was supported by BBSRC grant BB/F007566/1 to EC and a BBSRC studentship to RY.
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Yan, R., Simpson, P.J., Matthews, S.J. et al. Backbone 1H, 15N, 13C and Ile, Leu, Val methyl chemical shift assignments for the 33.5 kDa N-terminal domain of Candida albicans ALS1. Biomol NMR Assign 4, 187–190 (2010). https://doi.org/10.1007/s12104-010-9243-8
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DOI: https://doi.org/10.1007/s12104-010-9243-8