2ATG
NMR structure of Retrocyclin-2 in SDS
Summary for 2ATG
| Entry DOI | 10.2210/pdb2atg/pdb |
| NMR Information | BMRB: 6815 |
| Descriptor | Retrocyclin-2 (1 entity in total) |
| Functional Keywords | beta-sheet, circular peptide, laddered disulfide connectivity, antiviral protein |
| Total number of polymer chains | 1 |
| Total formula weight | 2046.63 |
| Authors | Daly, N.L.,Chen, Y.K.,Rosengren, K.J.,Marx, U.C.,Phillips, M.L.,Waring, A.J.,Wang, W.,Lehrer, R.I.,Craik, D.J. (deposition date: 2005-08-24, release date: 2005-09-06, Last modification date: 2024-11-13) |
| Primary citation | Daly, N.L.,Chen, Y.K.,Rosengren, K.J.,Marx, U.C.,Phillips, M.L.,Waring, A.J.,Wang, W.,Lehrer, R.I.,Craik, D.J. Retrocyclin-2: structural analysis of a potent anti-HIV theta-defensin Biochemistry, 46:9920-9928, 2007 Cited by PubMed Abstract: Retrocyclins are circular mini-defensins with significant potential as agents against human immunodeficiency virus, influenza A, and herpes simplex virus. Retrocyclins bind carbohydrate-containing surface molecules such as gp120 and CD4 with high affinity (Kd, 10-100 nM), promoting their localization on cell membranes. The structural features important for activity have yet to be fully elucidated, but here, we have determined the first three-dimensional structure of a retrocyclin, namely, one of the most potent forms, retrocyclin-2. In the presence of SDS micelles, a well-defined beta-hairpin braced by three disulfide bonds that defines the cystine ladder motif is present. By contrast, a well-defined structure could not be determined in aqueous solution, suggesting that the presence of SDS micelles stabilizes the extended conformation of retrocyclin-2. Translational diffusion measurements indicate that retrocyclin-2 interacts with the SDS micelles, and such a membrane-like interaction may be an important feature in the mechanism of action of these antimicrobial peptides. Analytical ultracentrifugation and the NMR data indicated that retrocyclin-2 self-associates to form a trimer in a concentration-dependent manner. The ability to self-associate may contribute to the high-affinity binding of retrocyclins for glycoproteins by increasing the valency and enhancing the ability of retrocyclins to cross-link cell surface glycoproteins. PubMed: 17685559DOI: 10.1021/bi700720e PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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