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Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-bindi...

Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-bindi...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5127623

Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site

About this item

Full title

Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site

Publisher

New York: Nature Publishing Group US

Journal title

Nature structural & molecular biology, 2016-10, Vol.23 (10), p.906-915

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

Crystal structures of HIV Env trimer with native glycosylation in complex with neutralizing antibodies reveal a glycan shield of high-mannose and complex-type N-glycan and indicate a path for germline-targeting vaccine design.
HIV-1 vaccine design is informed by structural studies elucidating mechanisms by which broadly neutralizing antibodies (...

Alternative Titles

Full title

Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5127623

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5127623

Other Identifiers

ISSN

1545-9993

E-ISSN

1545-9985

DOI

10.1038/nsmb.3291

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