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''' | + | {{Structure |
| + | |PDB= 1g6u |SIZE=350|CAPTION= <scene name='initialview01'>1g6u</scene>, resolution 1.48Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=TFA:TRIFLUOROACETYL GROUP'>TFA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF A DOMAIN SWAPPED DIMER''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1G6U is a [ | + | 1G6U is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. 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:// | + | 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: Protein complex]] | ||
[[Category: Bryson, J W.]] | [[Category: Bryson, J W.]] | ||
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[[Category: designed three helix bundle]] | [[Category: designed three helix bundle]] | ||
| - | ''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 11:19:00 2008'' |
Revision as of 09:19, 20 March 2008
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| , resolution 1.48Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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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