1q9l

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(New page: 200px<br /> <applet load="1q9l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q9l, resolution 2.28&Aring;" /> '''S25-2 Fab Unligande...)
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[[Image:1q9l.gif|left|200px]]<br />
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[[Image:1q9l.jpg|left|200px]]<br /><applet load="1q9l" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1q9l" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1q9l, resolution 2.28&Aring;" />
caption="1q9l, resolution 2.28&Aring;" />
'''S25-2 Fab Unliganded 2'''<br />
'''S25-2 Fab Unliganded 2'''<br />
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==About this Structure==
==About this Structure==
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1Q9L 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 ZN and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q9L OCA].
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1Q9L 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=ZN:'>ZN</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q9L OCA].
==Reference==
==Reference==
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[[Category: immunoglobulin]]
[[Category: immunoglobulin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:40:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:43:12 2008''

Revision as of 14:43, 15 February 2008


1q9l, resolution 2.28Å

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S25-2 Fab Unliganded 2

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

1Q9L 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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