1g6u
From Proteopedia
(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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| - | [[Image:1g6u.jpg|left|200px]]<br /><applet load="1g6u" size=" | + | [[Image:1g6u.jpg|left|200px]]<br /><applet load="1g6u" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g6u, resolution 1.48Å" /> | caption="1g6u, resolution 1.48Å" /> | ||
'''CRYSTAL STRUCTURE OF A DOMAIN SWAPPED DIMER'''<br /> | '''CRYSTAL STRUCTURE OF A DOMAIN SWAPPED DIMER'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Three-dimensional (3D) domain-swapped proteins are intermolecularly folded | + | 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== | ==About this Structure== | ||
| - | 1G6U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with SO4 and TFA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1G6U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=TFA:'>TFA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11171963 11171963] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Bryson, J | + | [[Category: Bryson, J W.]] |
| - | [[Category: DeGrado, W | + | [[Category: DeGrado, W F.]] |
[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
[[Category: Ghirlanda, G.]] | [[Category: Ghirlanda, G.]] | ||
[[Category: Gingery, M.]] | [[Category: Gingery, M.]] | ||
| - | [[Category: Ogihara, N | + | [[Category: Ogihara, N L.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: TFA]] | [[Category: TFA]] | ||
[[Category: designed three helix bundle]] | [[Category: designed three helix bundle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:44 2008'' |
Revision as of 10:46, 21 February 2008
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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 and 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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