1g6u

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|PDB= 1g6u |SIZE=350|CAPTION= <scene name='initialview01'>1g6u</scene>, resolution 1.48&Aring;
|PDB= 1g6u |SIZE=350|CAPTION= <scene name='initialview01'>1g6u</scene>, resolution 1.48&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=TFA:TRIFLUOROACETYL GROUP'>TFA</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TFA:TRIFLUOROACETYL+GROUP'>TFA</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g6u OCA], [http://www.ebi.ac.uk/pdbsum/1g6u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g6u RCSB]</span>
}}
}}
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[[Category: Gingery, M.]]
[[Category: Gingery, M.]]
[[Category: Ogihara, N L.]]
[[Category: Ogihara, N L.]]
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[[Category: SO4]]
 
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[[Category: TFA]]
 
[[Category: designed three helix bundle]]
[[Category: designed three helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:19:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:37:47 2008''

Revision as of 17:37, 30 March 2008


PDB ID 1g6u

Drag the structure with the mouse to rotate
, resolution 1.48Å
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
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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