1g6u
From Proteopedia
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- | [[ | + | ==CRYSTAL STRUCTURE OF A DOMAIN SWAPPED DIMER== |
+ | <StructureSection load='1g6u' size='340' side='right' caption='[[1g6u]], [[Resolution|resolution]] 1.48Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1g6u]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G6U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G6U FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TFA:TRIFLUOROACETIC+ACID'>TFA</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1g6u RCSB], [http://www.ebi.ac.uk/pdbsum/1g6u PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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<ref>PMID:11171963</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | + | </StructureSection> | |
[[Category: Bryson, J W.]] | [[Category: Bryson, J W.]] | ||
[[Category: DeGrado, W F.]] | [[Category: DeGrado, W F.]] |
Revision as of 14:31, 28 September 2014
CRYSTAL STRUCTURE OF A DOMAIN SWAPPED DIMER
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