2l2f

Publication Abstract from PubMed

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 Manalpha(1-2)Manalpha, its weak carbohydrate binding affinity to only one binding site is insufficient for conferring anti-HIV activity. Proteins 2011; (c) 2011 Wiley-Liss, Inc.

NMR solution structure of a cyanovirin homolog from wheat head blight fungus.,Matei E, Louis JM, Jee J, Gronenborn AM Proteins. 2011 Jan 18. doi: 10.1002/prot.22981. PMID:21365681^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.