1g6u
From Proteopedia
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[[Image:1g6u.jpg|left|200px]] | [[Image:1g6u.jpg|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF A DOMAIN SWAPPED DIMER''' | '''CRYSTAL STRUCTURE OF A DOMAIN SWAPPED DIMER''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G6U OCA]. | |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/11171963 11171963] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11171963 11171963] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Bryson, J W.]] | [[Category: Bryson, J W.]] | ||
[[Category: DeGrado, W F.]] | [[Category: DeGrado, W F.]] | ||
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[[Category: Gingery, M.]] | [[Category: Gingery, M.]] | ||
[[Category: Ogihara, N L.]] | [[Category: Ogihara, N L.]] | ||
| - | [[Category: | + | [[Category: Designed three helix bundle]] |
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Revision as of 14:12, 2 May 2008
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
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 Page seeded by OCA on Fri May 2 17:12:51 2008
