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3S3Z

Crystal Structure an Tandem Cyanovirin-N Dimer, CVN2L10

Summary for 3S3Z
Entry DOI10.2210/pdb3s3z/pdb
Related3S3Y
DescriptorTandem Cyanovirin-N Dimer CVN2L10, SODIUM ION (3 entities in total)
Functional Keywordscyanovirin-n, sugar-binding, gp120, engineered dimer, antiviral protein
Biological sourceNostoc ellipsosporum
More
Total number of polymer chains1
Total formula weight24045.19
Authors
Keeffe, J.R.,Bjorkman, P.J.,Mayo, S.L. (deposition date: 2011-05-18, release date: 2011-08-03, Last modification date: 2023-09-13)
Primary citationKeeffe, 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: 21799112
DOI: 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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