3LL1
Monomeric Griffithsin with a Single Gly-Ser Insertion and Mutations to Remove Residual Self-Association
Summary for 3LL1
| Entry DOI | 10.2210/pdb3ll1/pdb |
| Related | 2gty 2guc 2gud 2gue 2gux 2hyq 2hyr 2nu5 2nuo 3LKY 3LL0 3LL2 |
| Descriptor | Griffithsin, CHLORIDE ION (3 entities in total) |
| Functional Keywords | lectin, sugar-binding, anti-hiv, high mannose, man9, gp120, gp41, jacalin-related, mannose-binding, sugar binding protein |
| Biological source | Griffithsia (Red alga) |
| Total number of polymer chains | 1 |
| Total formula weight | 12663.08 |
| Authors | Moulaei, T.,Wlodawer, A. (deposition date: 2010-01-28, release date: 2010-10-06, Last modification date: 2023-09-06) |
| Primary citation | Moulaei, T.,Shenoy, S.R.,Giomarelli, B.,Thomas, C.,McMahon, J.B.,Dauter, Z.,O'Keefe, B.R.,Wlodawer, A. Monomerization of viral entry inhibitor griffithsin elucidates the relationship between multivalent binding to carbohydrates and anti-HIV activity. Structure, 18:1104-1115, 2010 Cited by PubMed Abstract: Mutations were introduced to the domain-swapped homodimer of the antiviral lectin griffithsin (GRFT). Whereas several single and double mutants remained dimeric, insertion of either two or four amino acids at the dimerization interface resulted in a monomeric form of the protein (mGRFT). Monomeric character of the modified proteins was confirmed by sedimentation equilibrium ultracentrifugation and by their high resolution X-ray crystal structures, whereas their binding to carbohydrates was assessed by isothermal titration calorimetry. Cell-based antiviral activity assays utilizing different variants of mGRFT indicated that the monomeric form of the lectin had greatly reduced activity against HIV-1, suggesting that the antiviral activity of GRFT stems from crosslinking and aggregation of viral particles via multivalent interactions between GRFT and oligosaccharides present on HIV envelope glycoproteins. Atomic resolution crystal structure of a complex between mGRFT and nonamannoside revealed that a single mGRFT molecule binds to two different nonamannoside molecules through all three carbohydrate-binding sites present on the monomer. PubMed: 20826337DOI: 10.1016/j.str.2010.05.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.97 Å) |
Structure validation
Download full validation report
