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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Cites
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Fine structure of human immunodeficiency virus (HIV) and immunolocalization of structural proteins
Gelderblom, H. R., Hausmann, E. H. S., Özel, M., Pauli, G., & Koch, M. A. (1987) · Virology · doi:10.1016/0042-6822(87)90449-1 · Cited by 521
Cited by
Barnes, C. O., West, A. P., Huey-Tubman, K. E., Hoffmann, M. A. G., Sharaf, N. G., Hoffman, P. R., Koranda, N., Gristick, H. B., Gaebler, C., Muecksch, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.025 · Cited by 795
Structural definition of a conserved neutralization epitope on HIV-1 gp120
Zhou, T., Xu, L., Dey, B., Hessell, A. J., Van Ryk, D., Xiang, S.-H., Yang, X., Zhang, M.-Y., Zwick, M. B., Arthos, J., et al. (2007) · Nature · doi:10.1038/nature05580 · Cited by 770
Self-citationUnraveling hot spots in binding interfaces: progress and challenges
DeLano, W. L. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00283-x · Cited by 767
Alternative molecular formats and therapeutic applications for bispecific antibodies
Spiess, C., Zhai, Q., & Carter, P. J. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.01.003 · Cited by 607
Structural and Functional Characterization of Disulfide Isoforms of the Human IgG2 Subclass
Dillon, T. M., Ricci, M. S., Vezina, C., Flynn, G. C., Liu, Y. D., Rehder, D. S., Plant, M., Henkle, B., Li, Y., Deechongkit, S., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709988200 · Cited by 291
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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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
