2GUE

Crystal structure of a complex of griffithsin with N-acetylglucosamine

2GUE の概要

• エントリーDOI: 10.2210/pdb2gue/pdb
• 関連するPDBエントリー: 2GTY 2GUC 2GUD 2GUX
• 分子名称: griffithsin, SULFATE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: griffithsin, lectins, domain swapping, mannose binding, hiv, sars, sugar binding protein
• 由来する生物種: Griffithsia
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27458.63

構造登録者

Ziolkowska, N.E.,Wlodawer, A. (登録日: 2006-04-29, 公開日: 2006-08-01, 最終更新日: 2024-10-30)

主引用文献

Ziolkowska, N.E.,O'keefe, B.R.,Mori, T.,Zhu, C.,Giomarelli, B.,Vojdani, F.,Palmer, K.E.,McMahon, J.B.,Wlodawer, A.
Domain-swapped structure of the potent antiviral protein griffithsin and its mode of carbohydrate binding.
Structure, 14:1127-1135, 2006

PubMed Abstract: The crystal structure of griffithsin, an antiviral lectin from the red alga Griffithsia sp., was solved and refined at 1.3 A resolution for the free protein and 0.94 A for a complex with mannose. Griffithsin molecules form a domain-swapped dimer, in which two beta strands of one molecule complete a beta prism consisting of three four-stranded sheets, with an approximate 3-fold axis, of another molecule. The structure of each monomer bears close resemblance to jacalin-related lectins, but its dimeric structure is unique. The structures of complexes of griffithsin with mannose and N-acetylglucosamine defined the locations of three almost identical carbohydrate binding sites on each monomer. We have also shown that griffithsin is a potent inhibitor of the coronavirus responsible for severe acute respiratory syndrome (SARS). Antiviral potency of griffithsin is likely due to the presence of multiple, similar sugar binding sites that provide redundant attachment points for complex carbohydrate molecules present on viral envelopes.

PubMed: 16843894
DOI: 10.1016/j.str.2006.05.017

実験手法

X-RAY DIFFRACTION (2.02 Å)