1shm
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1shm.gif|left|200px]] | [[Image:1shm.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1shm", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1shm| PDB=1shm | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Convergent solutions to VHH domain stabilization from natural and in vitro evolution''' | '''Convergent solutions to VHH domain stabilization from natural and in vitro evolution''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | + | 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://www.ncbi.nlm.nih.gov/pubmed/15826665 15826665] | 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: Protein complex]] | ||
[[Category: Bond, C J.]] | [[Category: Bond, C J.]] | ||
[[Category: Marsters, J C.]] | [[Category: Marsters, J C.]] | ||
[[Category: Sidhu, S S.]] | [[Category: Sidhu, S S.]] | ||
[[Category: Wiesmann, C.]] | [[Category: Wiesmann, C.]] | ||
| - | [[Category: | + | [[Category: Heavy chain variable domain]] |
| - | [[Category: | + | [[Category: Immunoglobulin]] |
| - | [[Category: | + | [[Category: Vhh domain]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:42:53 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:42, 3 May 2008
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
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 Sat May 3 08:42:53 2008
