1q9o: Difference between revisions
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==Overview== | ==Overview== | ||
High-resolution structures reveal how a germline antibody can recognize a | High-resolution structures reveal how a germline antibody can recognize a range of clinically relevant carbohydrate epitopes. The germline response to a carbohydrate immunogen can be critical to survivability, with selection for antibody gene segments that both confer protection against common pathogens and retain the flexibility to adapt to new disease organisms. We show here that antibody S25-2 binds several distinct inner-core epitopes of bacterial lipopolysaccharides (LPSs) by linking an inherited monosaccharide residue binding site with a subset of complementarity-determining regions (CDRs) of limited flexibility positioned to recognize the remainder of an array of different epitopes. This strategy allows germline antibodies to adapt to different epitopes while minimizing entropic penalties associated with the immobilization of labile CDRs upon binding of antigen, and provides insight into the link between the genetic origin of individual CDRs and their respective roles in antigen recognition. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Brade, H.]] | [[Category: Brade, H.]] | ||
[[Category: Brade, L.]] | [[Category: Brade, L.]] | ||
[[Category: Evans, S | [[Category: Evans, S V.]] | ||
[[Category: Kosma, P.]] | [[Category: Kosma, P.]] | ||
[[Category: MacKenzie, C | [[Category: MacKenzie, C R.]] | ||
[[Category: Nguyen, H | [[Category: Nguyen, H P.]] | ||
[[Category: Seto, N | [[Category: Seto, N O.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
[[Category: anti-carbohydrate]] | [[Category: anti-carbohydrate]] | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:19 2008'' | ||
Revision as of 15:37, 21 February 2008
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S45-18 Fab Unliganded
OverviewOverview
High-resolution structures reveal how a germline antibody can recognize a range of clinically relevant carbohydrate epitopes. The germline response to a carbohydrate immunogen can be critical to survivability, with selection for antibody gene segments that both confer protection against common pathogens and retain the flexibility to adapt to new disease organisms. We show here that antibody S25-2 binds several distinct inner-core epitopes of bacterial lipopolysaccharides (LPSs) by linking an inherited monosaccharide residue binding site with a subset of complementarity-determining regions (CDRs) of limited flexibility positioned to recognize the remainder of an array of different epitopes. This strategy allows germline antibodies to adapt to different epitopes while minimizing entropic penalties associated with the immobilization of labile CDRs upon binding of antigen, and provides insight into the link between the genetic origin of individual CDRs and their respective roles in antigen recognition.
About this StructureAbout this Structure
1Q9O is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Germline antibody recognition of distinct carbohydrate epitopes., Nguyen HP, Seto NO, MacKenzie CR, Brade L, Kosma P, Brade H, Evans SV, Nat Struct Biol. 2003 Dec;10(12):1019-25. Epub 2003 Nov 16. PMID:14625588
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