期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 79, 期 5, 页码 1538-1549出版社
WILEY-BLACKWELL
DOI: 10.1002/prot.22981
关键词
NMR solution structure; CVNH; lectin; antiviral protein; HIV
资金
- National Institutes of Health [GM080642]
- NIH [GM62116]
Members of the cyanovirin-N homolog (CVNH) lectin family are found in bacteria, fungi and plants. As part of our ongoing work on CVNH structure-function studies, we determined the high-resolution NMR solution structure of the homolog from the wheat head blight disease causing ascomycetous fungus Gibberella zeae (or Fusarium graminearum), hereafter called GzCVNH. Like cyanovirin-N (CV-N), GzCVNH comprises two tandem sequence repeats and the protein sequence exhibits 30% identity with CV-N. The overall structure is similar to those of other members of the CVNH family, with the conserved pseudo-symmetric halves of the structure, domains A and B, closely resembling recently determined structures of Tuber borchii, Neurospora crassa, and Ceratopteris richardii CVNH proteins. Although GzCVNH exhibits a similar glycan recognition profile to CV-N and specifically binds to Man alpha(1-2) Man alpha, its weak carbohydrate binding affinity to only one binding site is insufficient for conferring anti-HIV activity. Proteins 2011; 79: 1538-1549. (C) 2011 Wiley-Liss, Inc.
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