2KJL

NMR structures of a designed Cyanovirin-N homolog lectin; LKAMG

2KJL の概要

• エントリーDOI: 10.2210/pdb2kjl/pdb
• NMR情報: BMRB: 16339
• 分子名称: Cyanovirin-N homolog (1 entity in total)
• 機能のキーワード: cyanovirin-n, cvnh, lectin, sugar binding protein
• 由来する生物種: Tuber borchii,Neurospora crassa,Tuber borchii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12386.46

構造登録者

Koharudin, L.M.I.,Gronenborn, A.M. (登録日: 2009-05-31, 公開日: 2009-06-23, 最終更新日: 2024-05-01)

主引用文献

Koharudin, L.M.,Viscomi, A.R.,Jee, J.G.,Ottonello, S.,Gronenborn, A.M.
The evolutionarily conserved family of cyanovirin-N homologs: structures and carbohydrate specificity.
Structure, 16:570-584, 2008

PubMed Abstract: Solution structures for three members of the recently discovered cyanovirin-N (CV-N) homolog family of lectins have been determined. Cyanovirin-N homologs (CVNHs) from Tuber borchii, Ceratopteris richardii, and Neurospora crassa, representing each of the three phylogenetic groups, were selected. All proteins exhibit the same fold, and the overall structures resemble that of the founding member of the family, CV-N, albeit with noteworthy differences in loop conformation and detailed local structure. Since no data are available regarding the proteins' function or their natural ligands, extensive carbohydrate-binding studies were conducted. We delineated ligand-binding sites on all three proteins by nuclear magnetic resonance and identified which sugars interact by array screening. The number and location of binding sites vary for the three proteins, and different ligand specificities exist. Potential physiological roles for two family members, TbCVNH and NcCVNH, were probed in nutrition deprivation experiments that suggest a possible involvement of these proteins in lifestyle-related responses.

PubMed: 18400178
DOI: 10.1016/j.str.2008.01.015

実験手法

SOLUTION NMR