1oay: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1oay.jpg|left|200px]] | [[Image:1oay.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1oay", 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_1oay| PDB=1oay | SCENE= }} | |||
}} | |||
'''ANTIBODY MULTISPECIFICITY MEDIATED BY CONFORMATIONAL DIVERSITY''' | '''ANTIBODY MULTISPECIFICITY MEDIATED BY CONFORMATIONAL DIVERSITY''' | ||
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=1OAY OCA]. | |||
==Reference== | ==Reference== | ||
Antibody multispecificity mediated by conformational diversity., James LC, Roversi P, Tawfik DS, Science. 2003 Feb 28;299(5611):1362-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12610298 12610298] | Antibody multispecificity mediated by conformational diversity., James LC, Roversi P, Tawfik DS, Science. 2003 Feb 28;299(5611):1362-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12610298 12610298] | ||
[[Category: James, L C.]] | [[Category: James, L C.]] | ||
[[Category: Roversi, P.]] | [[Category: Roversi, P.]] | ||
[[Category: Tawfik, D.]] | [[Category: Tawfik, D.]] | ||
[[Category: | [[Category: Allergy]] | ||
[[Category: | [[Category: Antibody]] | ||
[[Category: | [[Category: Conformational diversity]] | ||
[[Category: | [[Category: Ige]] | ||
[[Category: | [[Category: Multispecificity]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:36:48 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 03:36, 3 May 2008
ANTIBODY MULTISPECIFICITY MEDIATED BY CONFORMATIONAL DIVERSITY
OverviewOverview
A single antibody was shown to adopt different binding-site conformations and thereby bind unrelated antigens. Analysis by both x-ray crystallography and pre-steady-state kinetics revealed an equilibrium between different preexisting isomers, one of which possessed a promiscuous, low-affinity binding site for aromatic ligands, including the immunizing hapten. A subsequent induced-fit isomerization led to high-affinity complexes with a deep and narrow binding site. A protein antigen identified by repertoire selection made use of an unrelated antibody isomer with a wide, shallow binding site. Conformational diversity, whereby one sequence adopts multiple structures and multiple functions, can increase the effective size of the antibody repertoire but may also lead to autoimmunity and allergy.
About this StructureAbout this Structure
Full crystallographic information is available from OCA.
ReferenceReference
Antibody multispecificity mediated by conformational diversity., James LC, Roversi P, Tawfik DS, Science. 2003 Feb 28;299(5611):1362-7. PMID:12610298 Page seeded by OCA on Sat May 3 03:36:48 2008