2a6d

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[[Image:2a6d.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_2a6d| PDB=2a6d | SCENE= }}
{{STRUCTURE_2a6d| PDB=2a6d | SCENE= }}
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'''Crystal structure analysis of the anti-arsonate germline antibody 36-65 in complex with a phage display derived dodecapeptide RLLIADPPSPRE'''
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===Crystal structure analysis of the anti-arsonate germline antibody 36-65 in complex with a phage display derived dodecapeptide RLLIADPPSPRE===
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==Overview==
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The limited primary antibody repertoire uses multiple mechanisms to account for the large number of potential antigens. In this issue of Immunity, Sethi et al. (2006) describe a new means for expanding the antibody repertoire, whereby a single antibody isomer binds diverse antigens at different regions of the binding site.
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The line below this paragraph, {{ABSTRACT_PUBMED_16618592}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16618592 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16618592}}
==About this Structure==
==About this Structure==
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[[Category: Fab]]
[[Category: Fab]]
[[Category: Germline]]
[[Category: Germline]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:39:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:56:25 2008''

Revision as of 08:56, 28 July 2008

Template:STRUCTURE 2a6d

Crystal structure analysis of the anti-arsonate germline antibody 36-65 in complex with a phage display derived dodecapeptide RLLIADPPSPRE

Template:ABSTRACT PUBMED 16618592

About this Structure

Full crystallographic information is available from OCA.

Reference

Multiple paths to multispecificity., Mariuzza RA, Immunity. 2006 Apr;24(4):359-61. PMID:16618592

Page seeded by OCA on Mon Jul 28 11:56:25 2008

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