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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/I1RM03_GIBZE I1RM03_GIBZE] | | [https://www.uniprot.org/uniprot/I1RM03_GIBZE I1RM03_GIBZE] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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<ref>PMID:21365681</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 2l2f" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
