1q9o: Difference between revisions

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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1q9o ConSurf].
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Revision as of 11:29, 7 February 2016

S45-18 Fab UnligandedS45-18 Fab Unliganded

Structural highlights

1q9o is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Nguyen HP, Seto NO, MacKenzie CR, Brade L, Kosma P, Brade H, Evans SV. Germline antibody recognition of distinct carbohydrate epitopes. Nat Struct Biol. 2003 Dec;10(12):1019-25. Epub 2003 Nov 16. PMID:14625588 doi:http://dx.doi.org/10.1038/nsb1014

1q9o, resolution 1.79Å

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OCA