2RP3

Solution Structure of Cyanovirin-N Domain B Mutant

2RP3 の概要

• エントリーDOI: 10.2210/pdb2rp3/pdb
• 関連するPDBエントリー: 2EZM
• 分子名称: Cyanovirin-N (1 entity in total)
• 機能のキーワード: cyanovirin-n, hiv-inactivating, gp120, monomer, no 3d domain-swapping, antiviral protein
• 由来する生物種: Nostoc ellipsosporum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10693.75

構造登録者

Matei, E.,Furey, W.,Gronenborn, A.M. (登録日: 2008-04-30, 公開日: 2008-08-19, 最終更新日: 2024-10-30)

主引用文献

Matei, E.,Furey, W.,Gronenborn, A.M.
Solution and crystal structures of a sugar binding site mutant of cyanovirin-N: no evidence of domain swapping
Structure, 16:1183-1194, 2008

PubMed Abstract: The cyanobacterial lectin Cyanovirin-N (CV-N) exhibits antiviral activity against HIV at a low nanomolar concentration by interacting with high-mannose oligosaccharides on the virus surface envelope glycoprotein gp120. Atomic structures of wild-type CV-N revealed a monomer in solution and a domain-swapped dimer in the crystal, with the monomer comprising two independent carbohydrate binding sites that individually bind with micromolar affinity to di- and trimannoses. In the mutant CVN(mutDB), the binding site on domain B was abolished and the protein was found to be completely inactive against HIV. We determined the solution NMR and crystal structures of this variant and characterized its sugar binding properties. In solution and the crystal, CVN(mutDB) is a monomer and no domain-swapping was observed. The protein binds to Man-3 and Man-9 with similar dissociation constants ( approximately 4 muM). This confirms that the nanomolar activity of wild-type CV-N is related to the multisite nature of the protein carbohydrate interaction.

PubMed: 18682220
DOI: 10.1016/j.str.2008.05.011

実験手法

SOLUTION NMR