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| [[Image:1q9k.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1q9k.png|left|200px]] |
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| {{STRUCTURE_1q9k| PDB=1q9k | SCENE= }} | | {{STRUCTURE_1q9k| PDB=1q9k | SCENE= }} |
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| '''S25-2 Fab Unliganded 1'''
| | ===S25-2 Fab Unliganded 1=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14625588}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14625588 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14625588}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Fab]] | | [[Category: Fab]] |
| [[Category: Immunoglobulin]] | | [[Category: Immunoglobulin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:02:21 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:29:55 2008'' |