2L2F
NMR Structure of GzCVNH (Gibberella zeae CVNH)
Summary for 2L2F
| Entry DOI | 10.2210/pdb2l2f/pdb |
| Descriptor | Cyanovirin-N HOMOLOG (1 entity in total) |
| Functional Keywords | cyanovirin-n homolog, lectin, carbohydrate binding protein, sugar binding protein |
| Biological source | Gibberella zeae |
| Total number of polymer chains | 1 |
| Total formula weight | 11673.41 |
| Authors | Matei, E.,Louis, J.M.,Jee, J.G.,Gronenborn, A.M. (deposition date: 2010-08-17, release date: 2011-03-23, Last modification date: 2024-05-01) |
| Primary citation | Matei, E.,Louis, J.M.,Jee, J.,Gronenborn, A.M. NMR solution structure of a cyanovirin homolog from wheat head blight fungus. Proteins, 79:1538-1549, 2011 Cited by PubMed Abstract: 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 Manα(1-2)Manα, its weak carbohydrate binding affinity to only one binding site is insufficient for conferring anti-HIV activity. PubMed: 21365681DOI: 10.1002/prot.22981 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
