1g6u
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(New page: 200px<br /><applet load="1g6u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g6u, resolution 1.48Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 22:49, 24 November 2007
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CRYSTAL STRUCTURE OF A DOMAIN SWAPPED DIMER
Overview
Three-dimensional (3D) domain-swapped proteins are intermolecularly folded, analogs of monomeric proteins; both are stabilized by the identical, interactions, but the individual domains interact intramolecularly in, monomeric proteins, whereas they form intermolecular interactions in 3D, domain-swapped structures. The structures and conditions of formation of, several domain-swapped dimers and trimers are known, but the formation of, higher order 3D domain-swapped oligomers has been less thoroughly studied., Here we contrast the structural consequences of domain swapping from two, designed three-helix bundles: one with an up-down-up topology, and the, other with an up-down-down topology. The up-down-up topology gives rise to, a domain-swapped dimer whose structure has been determined to 1.5 A, resolution by x-ray crystallography. In contrast, the domain-swapped, protein with an up-down-down topology forms fibrils as shown by electron, microscopy and dynamic light scattering. This demonstrates that design, principles can predict the oligomeric state of 3D domain-swapped, molecules, which should aid in the design of domain-swapped proteins and, biomaterials.
About this Structure
1G6U is a Protein complex structure of sequences from [1] with SO4 and TFA as ligands. Full crystallographic information is available from OCA.
Reference
Design of three-dimensional domain-swapped dimers and fibrous oligomers., Ogihara NL, Ghirlanda G, Bryson JW, Gingery M, DeGrado WF, Eisenberg D, Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1404-9. PMID:11171963
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