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Backbone 1H, 15N, 13C and Ile, Leu, Val methyl chemical shift assignments for the 33.5 kDa N-terminal domain of Candida albicans ALS1.

Authors
Type
Published Article
Journal
Biomolecular NMR Assignments
1874-270X
Publisher
Springer-Verlag
Publication Date
Volume
4
Issue
2
Pages
187–190
Identifiers
DOI: 10.1007/s12104-010-9243-8
PMID: 20556550
Source
Medline
License
Unknown

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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