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Volumn 300, Issue 5628, 2003, Pages 2065-2071

Antibody domain exchange is an immunological solution to carbohydrate cluster recognition

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CARBOHYDRATES; CRYSTAL STRUCTURE; DIMERS; IMMUNOLOGY; MUTAGENESIS; VIRUSES;

EID: 12444291017     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1083182     Document Type: Article
Times cited : (693)

References (70)
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    • Materials and methods are available as supporting material on Science Online.
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    • The "closed interface" refers to the interface between the swapped domain and the main domain that exists in both the monomer and the domain-swapped oligomer. The "hinge loop" is the segment of polypeptide chain that links the swapped domain and the main domain and adopts different conformations in the monomer and the domain-swapped oligomer. The "open interface" exists only in the domain-swapped oligomer, but not in the monomer. The interplay between these three factors (destabilization of the closed interface, conformational shift in the hinge loop, and an energetically favorable open interface) can promote domain swapping (21).
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    • Residues that are marked with a prime symbol (′) are from the second Fab molecule of the domain-exchanged Fab dimer.
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    • Gp120 coordinates represent the 2.2 Å crystal structure of core gp120 from the HxB2 strain of HIV-1 complexed to CD4 and Fab 17b (61).
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    • H′ interface was modeled in a manner similar to that described above.
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    • note
    • Supported by NIH Grants GM46192 (I.A.W.), AI33292 (D.R.B.), and a grant from IAVI (International Aids Vaccine Initiative) through the Neutralizing Antibody Consortium. We are grateful to the staff of the Stanford Synchrotron Radiation Laboratory (SSRL) Beamline 11-1 for assistance at the beamline; E. O. Saphire (The Scripps Research Institute) for the initial model of the carbohydrate on gp120; A. Heine (The Scripps Research Institute), R. Aguilar (The Scripps Research Institute), S. Church (The Scripps Research Institute) and B. Matthews (Oxford Glycobiology Institute, UK) for expert technical assistance; R. Lerner (The Scripps Research Institute), J. Binley (The Scripps Research Institute), and M. Crispin (Oxford Glycobiology Institute, UK) for helpful discussion and comments. This is publication 15508-MB from The Scripps Research Institute. Coordinates have been deposited in the Protein Data Bank (codes 1OM3, 1OP3, and 1OP5) and will be released immediately upon publication.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.