2bjm: Difference between revisions
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[[Image:2bjm.gif|left|200px]] | [[Image:2bjm.gif|left|200px]] | ||
'''SPE7:ANTHRONE COMPLEX''' | {{Structure | ||
|PDB= 2bjm |SIZE=350|CAPTION= <scene name='initialview01'>2bjm</scene>, resolution 2.150Å | |||
|SITE= <scene name='pdbsite=AC1:Anf+Binding+Site+For+Chain+H'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=ANF:ANTHRONE'>ANF</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''SPE7:ANTHRONE COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2BJM is a [ | 2BJM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BJM OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16129832 16129832] | ||
[[Category: Rattus rattus]] | [[Category: Rattus rattus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: promiscuity]] | [[Category: promiscuity]] | ||
''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 16:02:47 2008'' | ||
Revision as of 14:02, 20 March 2008
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| 2bjm, resolution 2.150Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | ANF | ||||||||||||
| 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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