2bjm
From Proteopedia
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'''SPE7:ANTHRONE COMPLEX''' | '''SPE7:ANTHRONE COMPLEX''' | ||
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[[Category: James, L C.]] | [[Category: James, L C.]] | ||
[[Category: Tawfik, D S.]] | [[Category: Tawfik, D S.]] | ||
| - | [[Category: | + | [[Category: Antibody]] |
| - | [[Category: | + | [[Category: Encounter complex]] |
| - | [[Category: | + | [[Category: Multispecificity]] |
| - | [[Category: | + | [[Category: Promiscuity]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:22:51 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:22, 3 May 2008
SPE7:ANTHRONE COMPLEX
Overview
Induced fit is a predominant phenomenon in protein-ligand interactions, yet it is invariably attributed without establishing the existence, let alone the structure, of the initial, low-affinity encounter complex. We determined the crystal structure of the encounter complex on the pathway of ligand binding by IgE antibody SPE7. We show that this complex is formed by a wide range of ligands that initially bind with identical affinity. Nonspecific ligands rapidly dissociate, whereupon the antibody isomerizes to a nonbinding isomer. Specific ligand complexes, however, slowly isomerize to give a high-affinity complex. This isomerization involves backbone and side-chain rearrangements of up to 14 A and the formation of specific hydrogen bonds. The postbinding conformational switch, combined with the prebinding isomerization to an energetically favorable nonbinding isomer, results in a "kinetic discrimination" mechanism that mediates selective binding, by a factor of >10(3), between highly related ligands that initially bind with the same affinity. This model may apply to proteins that bind multiple ligands in a specific manner or other proteins that, although capable of binding many ligands, are activated by only a few.
About this Structure
2BJM is a Single protein structure of sequence from Rattus rattus. Full crystallographic information is available from OCA.
Reference
Structure and kinetics of a transient antibody binding intermediate reveal a kinetic discrimination mechanism in antigen recognition., James LC, Tawfik DS, Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12730-5. Epub 2005 Aug 29. PMID:16129832 Page seeded by OCA on Sat May 3 20:22:51 2008
