1ggc
From Proteopedia
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| - | [[Image:1ggc.gif|left|200px]] | + | [[Image:1ggc.gif|left|200px]] |
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| - | '''MAJOR ANTIGEN-INDUCED DOMAIN REARRANGEMENTS IN AN ANTIBODY''' | + | {{Structure |
| + | |PDB= 1ggc |SIZE=350|CAPTION= <scene name='initialview01'>1ggc</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''MAJOR ANTIGEN-INDUCED DOMAIN REARRANGEMENTS IN AN ANTIBODY''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GGC is a [ | + | 1GGC is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GGC OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8069628 8069628] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Takimoto-Kamimura, M.]] | [[Category: Takimoto-Kamimura, M.]] | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:22:42 2008'' |
Revision as of 09:22, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
MAJOR ANTIGEN-INDUCED DOMAIN REARRANGEMENTS IN AN ANTIBODY
Overview
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 Structure
1GGC is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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 Thu Mar 20 11:22:42 2008
