1q9v

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(New page: 200px<br /> <applet load="1q9v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q9v, resolution 1.73&Aring;" /> '''S25-2- Kdo monosacc...)
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[[Image:1q9v.gif|left|200px]]<br />
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[[Image:1q9v.gif|left|200px]]<br /><applet load="1q9v" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1q9v" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1q9v, resolution 1.73&Aring;" />
caption="1q9v, resolution 1.73&Aring;" />
'''S25-2- Kdo monosaccharide complex'''<br />
'''S25-2- Kdo monosaccharide complex'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1Q9V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with KDO, MG and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q9V OCA].
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1Q9V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=KDO:'>KDO</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q9V OCA].
==Reference==
==Reference==
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[[Category: Brade, H.]]
[[Category: Brade, H.]]
[[Category: Brade, L.]]
[[Category: Brade, L.]]
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[[Category: Evans, S.V.]]
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[[Category: Evans, S V.]]
[[Category: Kosma, P.]]
[[Category: Kosma, P.]]
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[[Category: MacKenzie, C.R.]]
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[[Category: MacKenzie, C R.]]
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[[Category: Nguyen, H.P.]]
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[[Category: Nguyen, H P.]]
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[[Category: Seto, N.O.]]
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[[Category: Seto, N O.]]
[[Category: KDO]]
[[Category: KDO]]
[[Category: MG]]
[[Category: MG]]
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[[Category: protein-carbohydrate complex]]
[[Category: protein-carbohydrate complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:40:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:23 2008''

Revision as of 12:37, 21 February 2008


1q9v, resolution 1.73Å

Drag the structure with the mouse to rotate

S25-2- Kdo monosaccharide complex

Overview

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

1Q9V is a Protein complex structure of sequences from Mus musculus with , and as ligands. Full crystallographic information is available from OCA.

Reference

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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