2bjm
From Proteopedia
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| - | [[Image:2bjm.gif|left|200px]]<br /><applet load="2bjm" size=" | + | [[Image:2bjm.gif|left|200px]]<br /><applet load="2bjm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bjm, resolution 2.150Å" /> | caption="2bjm, resolution 2.150Å" /> | ||
'''SPE7:ANTHRONE COMPLEX'''<br /> | '''SPE7:ANTHRONE COMPLEX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BJM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with ANF as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Anf Binding Site For Chain H'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2BJM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with <scene name='pdbligand=ANF:'>ANF</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Anf+Binding+Site+For+Chain+H'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BJM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: promiscuity]] | [[Category: promiscuity]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:24:56 2008'' |
Revision as of 08:24, 3 February 2008
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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 with as ligand. Known structural/functional Site: . 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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