2guc
From Proteopedia
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Crystal structure of a complex of griffithsin with mannose at 1.78 A resolution.
Overview
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.
About this Structure
2GUC is a Single protein structure of sequence from Griffithsia with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Domain-swapped structure of the potent antiviral protein griffithsin and its mode of carbohydrate binding., Ziolkowska NE, O'Keefe BR, Mori T, Zhu C, Giomarelli B, Vojdani F, Palmer KE, McMahon JB, Wlodawer A, Structure. 2006 Jul;14(7):1127-35. PMID:16843894
Page seeded by OCA on Fri Feb 15 17:28:57 2008
Categories: Griffithsia | Single protein | Wlodawer, A. | Ziolkowska, N.E. | ACE | EDO | MAN | SO4 | Domain swapping | Griffithsin | Hiv | Lectins | Mannose binding | Sars
