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2bjm
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjm OCA], [http://www.ebi.ac.uk/pdbsum/2bjm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bjm RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: James, L C.]] | [[Category: James, L C.]] | ||
[[Category: Tawfik, D S.]] | [[Category: Tawfik, D S.]] | ||
| - | [[Category: ANF]] | ||
[[Category: antibody]] | [[Category: antibody]] | ||
[[Category: encounter complex]] | [[Category: encounter complex]] | ||
| Line 30: | Line 32: | ||
[[Category: promiscuity]] | [[Category: promiscuity]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:07:25 2008'' |
Revision as of 23:07, 30 March 2008
| |||||||
| , resolution 2.150Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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