3S3Z
Crystal Structure an Tandem Cyanovirin-N Dimer, CVN2L10
Summary for 3S3Z
| Entry DOI | 10.2210/pdb3s3z/pdb |
| Related | 3S3Y |
| Descriptor | Tandem Cyanovirin-N Dimer CVN2L10, SODIUM ION (3 entities in total) |
| Functional Keywords | cyanovirin-n, sugar-binding, gp120, engineered dimer, antiviral protein |
| Biological source | Nostoc ellipsosporum More |
| Total number of polymer chains | 1 |
| Total formula weight | 24045.19 |
| Authors | Keeffe, J.R.,Bjorkman, P.J.,Mayo, S.L. (deposition date: 2011-05-18, release date: 2011-08-03, Last modification date: 2024-11-20) |
| Primary citation | Keeffe, J.R.,Gnanapragasam, P.N.,Gillespie, S.K.,Yong, J.,Bjorkman, P.J.,Mayo, S.L. Designed oligomers of cyanovirin-N show enhanced HIV neutralization. Proc.Natl.Acad.Sci.USA, 108:14079-14084, 2011 Cited by PubMed Abstract: Cyanovirin-N (CV-N) is a small, cyanobacterial lectin that neutralizes many enveloped viruses, including human immunodeficiency virus type I (HIV-1). This antiviral activity is attributed to two homologous carbohydrate binding sites that specifically bind high mannose glycosylation present on envelope glycoproteins such as HIV-1 gp120. We created obligate CV-N oligomers to determine whether increasing the number of binding sites has an effect on viral neutralization. A tandem repeat of two CV-N molecules (CVN(2)) increased HIV-1 neutralization activity by up to 18-fold compared to wild-type CV-N. In addition, the CVN(2) variants showed extensive cross-clade reactivity and were often more potent than broadly neutralizing anti-HIV antibodies. The improvement in activity and broad cross-strain HIV neutralization exhibited by these molecules holds promise for the future therapeutic utility of these and other engineered CV-N variants. PubMed: 21799112DOI: 10.1073/pnas.1108777108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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