2GTY

Crystal structure of unliganded griffithsin

Summary for 2GTY

• Entry DOI: 10.2210/pdb2gty/pdb
• Related: 2GUC 2GUD 2GUE 2GUX
• Descriptor: Griffithsin, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: griffithsin, lectins, domain swapping, mannose binding, hiv, sars, sugar binding protein
• Biological source: Griffithsia
• Total number of polymer chains: 2
• Total formula weight: 26594.60

Authors

Ziolkowska, N.E.,Wlodawer, A. (deposition date: 2006-04-28, release date: 2006-08-01, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.3 Å)