1shm

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{{Seed}}
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{{STRUCTURE_1shm| PDB=1shm | SCENE= }}
{{STRUCTURE_1shm| PDB=1shm | SCENE= }}
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'''Convergent solutions to VHH domain stabilization from natural and in vitro evolution'''
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===Convergent solutions to VHH domain stabilization from natural and in vitro evolution===
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==Overview==
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The diversity of natural antibodies is limited by the genetic mechanisms that engender diversity and the functional requirements of antigen binding. Using an in vitro-evolved autonomous heavy chain variable domain (V(H)H-RIG), we have investigated the limits of structurally-tolerated diversity in the three complementarity-determining regions and a fourth loop within the third framework region. We determined the X-ray crystal structure of the V(H)H-RIG domain at 1.9A resolution and used it to guide the design of phage-displayed libraries encompassing the four loops. The libraries were subjected to selections for structural stability, and a database of structurally-tolerated sequences was compiled from the sequences of approximately 1000 unique clones. The results reveal that all four loops accommodate significantly greater diversity than is observed in nature. Thus, it appears that most sequence biases in the natural immune repertoire arise from factors other than structural constraints and, consequently, it should be possible to enhance the functions of antibodies significantly through in vitro evolution.
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The line below this paragraph, {{ABSTRACT_PUBMED_15826665}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15826665 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15826665}}
==About this Structure==
==About this Structure==
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[[Category: Immunoglobulin]]
[[Category: Immunoglobulin]]
[[Category: Vhh domain]]
[[Category: Vhh domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:42:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:18:08 2008''

Revision as of 12:18, 27 July 2008

Image:1shm.png

Template:STRUCTURE 1shm

Convergent solutions to VHH domain stabilization from natural and in vitro evolution

Template:ABSTRACT PUBMED 15826665

About this Structure

Full crystallographic information is available from OCA.

Reference

A structure-based database of antibody variable domain diversity., Bond CJ, Wiesmann C, Marsters JC Jr, Sidhu SS, J Mol Biol. 2005 May 6;348(3):699-709. PMID:15826665

Page seeded by OCA on Sun Jul 27 15:18:08 2008

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