1L5E

The domain-swapped dimer of CV-N in solution

1L5E の概要

• エントリーDOI: 10.2210/pdb1l5e/pdb
• 関連するPDBエントリー: 1L5B 2EZM 3EZM
• 分子名称: Cyanovirin-N (1 entity in total)
• 機能のキーワード: 3d domain-swapping, cyanovirin-n, protein folding, antiviral protein
• 由来する生物種: Nostoc ellipsosporum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22044.18

構造登録者

Barrientos, L.G.,Louis, J.M.,Botos, I.,Mori, T.,Han, Z.,O'Keefe, B.R.,Boyd, M.R.,Wlodawer, A.,Gronenborn, A.M. (登録日: 2002-03-06, 公開日: 2002-06-05, 最終更新日: 2024-10-30)

主引用文献

Barrientos, L.G.,Louis, J.M.,Botos, I.,Mori, T.,Han, Z.,O'Keefe, B.R.,Boyd, M.R.,Wlodawer, A.,Gronenborn, A.M.
The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures.
Structure, 10:673-686, 2002

PubMed Abstract: The structure of the potent HIV-inactivating protein cyanovirin-N was previously found by NMR to be a monomer in solution and a domain-swapped dimer by X-ray crystallography. Here we demonstrate that, in solution, CV-N can exist both in monomeric and in domain-swapped dimeric form. The dimer is a metastable, kinetically trapped structure at neutral pH and room temperature. Based on orientational NMR constraints, we show that the domain-swapped solution dimer is similar to structures in two different crystal forms, exhibiting solely a small reorientation around the hinge region. Mutation of the single proline residue in the hinge to glycine significantly stabilizes the protein in both its monomeric and dimeric forms. By contrast, mutation of the neighboring serine to proline results in an exclusively dimeric protein, caused by a drastic destabilization of the monomer.

PubMed: 12015150
DOI: 10.1016/S0969-2126(02)00758-X

実験手法

SOLUTION NMR