1shm
From Proteopedia
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| - | [[Image:1shm.gif|left|200px]] | + | [[Image:1shm.gif|left|200px]] |
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| - | '''Convergent solutions to VHH domain stabilization from natural and in vitro evolution''' | + | {{Structure |
| + | |PDB= 1shm |SIZE=350|CAPTION= <scene name='initialview01'>1shm</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Convergent solutions to VHH domain stabilization from natural and in vitro evolution''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SHM is a [ | + | 1SHM is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHM OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15826665 15826665] |
[[Category: Lama glama]] | [[Category: Lama glama]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: vhh domain]] | [[Category: vhh domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:05:02 2008'' |
Revision as of 12:05, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Convergent solutions to VHH domain stabilization from natural and in vitro evolution
Overview
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.
About this Structure
1SHM is a Protein complex structure of sequences from Lama glama. 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
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