The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Crystal Structure of a Neutralizing Human IgG Against HIV-1: A Template for Vaccine Design
Abstract
We present the crystal structure at 2.7 angstrom resolution of the human antibody IgG1 b12. Antibody b12 recognizes the CD4-binding site of human immunodeficiency virus–1 (HIV-1) gp120 and is one of only two known antibodies against gp120 capable of broad and potent neutralization of primary HIV-1 isolates. A key feature of the antibody-combining site is the protruding, finger-like long CDR H3 that can penetrate the recessed CD4-binding site of gp120. A docking model of b12 and gp120 reveals severe structural constraints that explain the extraordinary challenge in eliciting effective neutralizing antibodies similar to b12. The structure, together with mutagenesis studies, provides a rationale for the extensive cross-reactivity of b12 and a valuable framework for the design of HIV-1 vaccines capable of eliciting b12-like activity.
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Self-citationUnraveling hot spots in binding interfaces: progress and challenges
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The Fab region of IgG impairs the internalization pathway of FcRn upon Fc engagement
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Metadata
- Authors
- Saphire, E. O., Parren, P. W. H. I., Pantophlet, R., Zwick, M. B., Morris, G. M., Rudd, P. M., Dwek, R. A., Stanfield, R. L., Burton, D. R., & Wilson, I. A.
- Venue
- Science
- Published
- 2001-08-10
- Volume
- 293
- Issue
- 5532
- Pages
- 1155-1159
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2096387523
- Cited by
- 942
- References
- 2
- FWCI
- 10.06
- Type
- journal article
- Language
- en
- Open access
- closed
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