2GUE: Crystal Structure Of A Complex Of Griffithsin With N-Acetylglucosamine

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.
PDB ID: 2GUEDownload
MMDB ID: 106398
PDB Deposition Date: 2006/4/29
Updated in MMDB: 2013/01
Experimental Method:
x-ray diffraction
Resolution: 2.02  Å
Source Organism:
Similar Structures:
Biological Unit for 2GUE: dimeric; determined by author and by software (PISA)
Molecular Components in 2GUE
Label Count Molecule
Proteins (2 molecules)
Molecule annotation
Chemicals (27 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB