2hfg: Difference between revisions

Revision as of 11:17, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2hfg.png

Template:STRUCTURE 2hfg

Crystal structure of hBR3 bound to CB3s-FabCrystal structure of hBR3 bound to CB3s-Fab

Template:ABSTRACT PUBMED 16840730

About this StructureAbout this Structure

2HFG is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Synthetic anti-BR3 antibodies that mimic BAFF binding and target both human and murine B cells., Lee CV, Hymowitz SG, Wallweber HJ, Gordon NC, Billeci KL, Tsai SP, Compaan DM, Yin J, Gong Q, Kelley RF, DeForge LE, Martin F, Starovasnik MA, Fuh G, Blood. 2006 Nov 1;108(9):3103-11. Epub 2006 Jul 13. PMID:16840730

Page seeded by OCA on Tue Jul 29 11:16:55 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of hBR3 bound to CB3s-Fab'''
+===Crystal structure of hBR3 bound to CB3s-Fab===
-==Overview==
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-BR3, which is expressed on all mature B cells, is a specific receptor for the B-cell survival and maturation factor BAFF (B-cell-activating factor belonging to the tumor necrosis factor [TNF] family). In order to investigate the consequences of targeting BR3 in murine models and to assess the potential of BR3 antibodies as human therapeutics, synthetic antibody phage libraries were employed to identify BAFF-blocking antibodies cross-reactive to murine and human BR3, which share 52% identity in their extracellular domains. We found an antibody, CB1, which exhibits muM affinity for murine BR3 and very weak affinity for the human receptor. CB3s, an affinity-matured variant of CB1, has sub-nM affinity for BR3 from both species. Alanine scanning and crystallographic structural analysis of the CB3s/BR3 complex reveal that CB3s mimics BAFF by interacting with a similar region of the BR3 surface. Despite this similarity in binding epitopes, CB1 variants antagonize BAFF-dependent human B-cell proliferation in vitro and are effective at reducing murine B-cell populations in vivo, showing significant promise as therapeutics for human B-cell-mediated diseases.
+The line below this paragraph, {{ABSTRACT_PUBMED_16840730}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Fab fragment]]
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