1cdc
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(New page: 200px<br /><applet load="1cdc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cdc, resolution 2.0Å" /> '''CD2, N-TERMINAL DOMAI...)
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Revision as of 10:14, 20 November 2007
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CD2, N-TERMINAL DOMAIN (1-99), TRUNCATED FORM
Overview
When expressed as part of a glutathione S-transferase fusion protein the, NH2-terminal domain of the lymphocyte cell adhesion molecule CD2 is shown, to adopt two different folds. The immunoglobulin superfamily structure of, the major (85%) monomeric component has previously been determined by both, x-ray crystallography and NMR spectroscopy. We now describe the structure, of a second, dimeric, form present in about 15% of recombinant CD2, molecules. After denaturation and refolding in the absence of the fusion, partner, dimeric CD2 is converted to monomer, illustrating that the, dimeric form represents a metastable folded state. The crystal structure, of this dimeric form, refined to 2.0-A resolution, reveals two domains, with overall similarity to the IgSF fold found in the monomer. However, in, the dimer each domain is formed by the intercalation of two polypeptide, chains. Hence each domain represents a distinct folding unit that can, assemble in two different ways. In the dimer the two domains fold around a, hydrophilic interface believed to mimic the cell adhesion interaction at, the cell surface, and the formation of dimer can be regulated by mutating, single residues at this interface. This unusual misfolded form of the, protein, which appears to result from inter- rather than intramolecular, interactions being favored by an intermediate structure formed during the, folding process, illustrates that evolution of protein oligomers is, possible from the sequence for a single protein domain.
About this Structure
1CDC is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
One sequence, two folds: a metastable structure of CD2., Murray AJ, Lewis SJ, Barclay AN, Brady RL, Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7337-41. PMID:7638192
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