1ggb: Difference between revisions
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'''MAJOR ANTIGEN-INDUCED DOMAIN REARRANGEMENTS IN AN ANTIBODY''' | '''MAJOR ANTIGEN-INDUCED DOMAIN REARRANGEMENTS IN AN ANTIBODY''' | ||
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==About this Structure== | ==About this Structure== | ||
1GGB is a [[Protein complex]] structure | 1GGB is a [[Protein complex]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GGB OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Takimoto-Kamimura, M.]] | [[Category: Takimoto-Kamimura, M.]] | ||
[[Category: Wilson, I A.]] | [[Category: Wilson, I A.]] | ||
[[Category: | [[Category: Immunoglobulin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:31:34 2008'' | |||
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Revision as of 17:31, 2 May 2008
MAJOR ANTIGEN-INDUCED DOMAIN REARRANGEMENTS IN AN ANTIBODY
OverviewOverview
BACKGROUND: Recent structural results have shown that antibodies use an induced fit mechanism to recognize and bind their antigens. Here we present the crystallographically determined structure of an Fab directed against an HIV-1 peptide (Fab 50.1) in the unliganded state and compare it with the peptide-bound structure. We perform a detailed analysis of the components that contribute to enhanced antigen binding and recognition. RESULTS: Induced fit of Fab 50.1 to its peptide antigen involves a substantial rearrangement of the third complementarity determining region loop of the heavy chain (H3), as well as a large rotation of the variable heavy (VH) chain relative to the variable light (VL) chain. Analysis of other Fab structures suggests that the extent of the surface area buried at the VL-VH interface correlates with the ability to alter antibody quaternary structure by reorientation of the VL-VH domains. CONCLUSION: Fab 50.1 exhibits the largest conformational changes yet observed in a single antibody. These can be attributed to the flexibility of the variable region. Comparisons of new data with previous examples lend to the general conclusion that a small VL-VH interface, due in part to a short H3 loop, permits substantial alterations to the antigen-binding pocket. This has major implications for the prediction, engineering and design of antibody-combining sites.
About this StructureAbout this Structure
1GGB is a Protein complex structure. Full crystallographic information is available from OCA.
ReferenceReference
Major antigen-induced domain rearrangements in an antibody., Stanfield RL, Takimoto-Kamimura M, Rini JM, Profy AT, Wilson IA, Structure. 1993 Oct 15;1(2):83-93. PMID:8069628 Page seeded by OCA on Fri May 2 17:31:34 2008