2L2F

NMR Structure of GzCVNH (Gibberella zeae CVNH)

2L2F の概要

• エントリーDOI: 10.2210/pdb2l2f/pdb
• 分子名称: Cyanovirin-N HOMOLOG (1 entity in total)
• 機能のキーワード: cyanovirin-n homolog, lectin, carbohydrate binding protein, sugar binding protein
• 由来する生物種: Gibberella zeae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11673.41

構造登録者

Matei, E.,Louis, J.M.,Jee, J.G.,Gronenborn, A.M. (登録日: 2010-08-17, 公開日: 2011-03-23, 最終更新日: 2024-05-01)

主引用文献

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

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: 21365681
DOI: 10.1002/prot.22981

実験手法

SOLUTION NMR