1e6o: Difference between revisions
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'''CRYSTAL STRUCTURE OF FAB13B5 AGAINST HIV-1 CAPSID PROTEIN P24''' | {{Structure | ||
|PDB= 1e6o |SIZE=350|CAPTION= <scene name='initialview01'>1e6o</scene>, resolution 1.8Å | |||
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'''CRYSTAL STRUCTURE OF FAB13B5 AGAINST HIV-1 CAPSID PROTEIN P24''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E6O is a [ | 1E6O is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E6O OCA]. | ||
==Reference== | ==Reference== | ||
Mutual conformational adaptations in antigen and antibody upon complex formation between an Fab and HIV-1 capsid protein p24., Monaco-Malbet S, Berthet-Colominas C, Novelli A, Battai N, Piga N, Cheynet V, Mallet F, Cusack S, Structure. 2000 Oct 15;8(10):1069-77. PMID:[http:// | Mutual conformational adaptations in antigen and antibody upon complex formation between an Fab and HIV-1 capsid protein p24., Monaco-Malbet S, Berthet-Colominas C, Novelli A, Battai N, Piga N, Cheynet V, Mallet F, Cusack S, Structure. 2000 Oct 15;8(10):1069-77. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11080628 11080628] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: p24]] | [[Category: p24]] | ||
''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 10:50:40 2008'' | ||
Revision as of 11:50, 20 March 2008
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CRYSTAL STRUCTURE OF FAB13B5 AGAINST HIV-1 CAPSID PROTEIN P24
OverviewOverview
BACKGROUND: Elucidating the structural basis of antigen-antibody recognition ideally requires a structural comparison of free and complexed components. To this end we have studied a mouse monoclonal antibody, denoted 13B5, raised against p24, the capsid protein of HIV-1. We have previously described the first crystal structure of intact p24 as visualized in the Fab13B5-p24 complex. Here we report the structure of the uncomplexed Fab13B5 at 1.8 A resolution and analyze the Fab-p24 interface and the conformational changes occurring upon complex formation. RESULTS: Fab13B5 recognizes a nearly continuous epitope comprising a helix-turn-helix motif in the C-terminal domain of p24. Only 4 complementarity-determining regions (CDRs) are in contact with p24 with most interactions being by the heavy chain. Comparison of the free and complexed Fab reveals that structural changes upon binding are localized to a few side chains of CDR-H1 and -H2 but involve a larger, concerted displacement of CDR-H3. Antigen binding is also associated with an 8 degrees relative rotation of the heavy and light chain variable regions. In p24, small conformational changes localized to the turn between the two helices comprising the epitope result from Fab binding. CONCLUSIONS: The relatively small area of contact between Fab13B5 and p24 may be related to the fact that the epitope is a continuous peptide rather than a more complex protein surface and correlates with a relatively low affinity of antigen and antibody. Despite this, a significant quaternary structural change occurs in the Fab upon complex formation, with additional smaller adaptations of both antigen and antibody.
About this StructureAbout this Structure
1E6O is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Mutual conformational adaptations in antigen and antibody upon complex formation between an Fab and HIV-1 capsid protein p24., Monaco-Malbet S, Berthet-Colominas C, Novelli A, Battai N, Piga N, Cheynet V, Mallet F, Cusack S, Structure. 2000 Oct 15;8(10):1069-77. PMID:11080628
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