1cqk
From Proteopedia
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| - | [[Image:1cqk.jpg|left|200px]] | + | [[Image:1cqk.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE CH3 DOMAIN FROM THE MAK33 ANTIBODY''' | + | {{Structure |
| + | |PDB= 1cqk |SIZE=350|CAPTION= <scene name='initialview01'>1cqk</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF THE CH3 DOMAIN FROM THE MAK33 ANTIBODY''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CQK is a [ | + | 1CQK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQK OCA]. |
==Reference== | ==Reference== | ||
| - | Folding and association of the antibody domain CH3: prolyl isomerization preceeds dimerization., Thies MJ, Mayer J, Augustine JG, Frederick CA, Lilie H, Buchner J, J Mol Biol. 1999 Oct 15;293(1):67-79. PMID:[http:// | + | Folding and association of the antibody domain CH3: prolyl isomerization preceeds dimerization., Thies MJ, Mayer J, Augustine JG, Frederick CA, Lilie H, Buchner J, J Mol Biol. 1999 Oct 15;293(1):67-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10512716 10512716] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''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 10:27:42 2008'' |
Revision as of 08:27, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE CH3 DOMAIN FROM THE MAK33 ANTIBODY
Overview
The simplest naturally occurring model system for studying immunoglobulin folding and assembly is the non-covalent homodimer formed by the C-terminal domains (CH3) of the heavy chains of IgG. Here, we describe the structure of recombinant CH3 dimer as determined by X-ray crystallography and an analysis of the folding pathway of this protein.Under conditions where prolyl isomerization does not contribute to the folding kinetics, formation of the beta-sandwich structure is the rate-limiting step. beta-Sheet formation of CH3 is a slow process, even compared to other antibody domains, while the subsequent association of the folded monomers is fast. After long-time denaturation, the majority of the unfolded CH3 molecules reaches the native state in two serial reactions, involving the re-isomerization of the Pro35-peptide bond to the cis configuration. The species with the wrong isomer accumulate as a monomeric intermediate. Importantly, the isomerization to the correct cis configuration is the prerequisite for dimerization of the CH3 domain. In contrast, in the Fab fragment of the same antibody, prolyl isomerization occurs after dimerization demonstrating that within one protein, comprised of highly homologous domains, both the kinetics of beta-sandwich formation and the stage at which prolyl isomerization occurs during the folding process can be completely different.
About this Structure
1CQK is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Folding and association of the antibody domain CH3: prolyl isomerization preceeds dimerization., Thies MJ, Mayer J, Augustine JG, Frederick CA, Lilie H, Buchner J, J Mol Biol. 1999 Oct 15;293(1):67-79. PMID:10512716
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