This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1u3z
From Proteopedia
Revision as of 21:50, 29 September 2014 by OCA (Talk | contribs)
1u3z is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Protein-protein interactions govern a wide range of cellular processes. Molecular recognition responsible for homodimerization and heterodimerization in the rel/NF-kappaB family of eukaryotic transcription factors relies on a small cluster of hydrophobic residues. We have carried out a structural analysis of six NF-kappaB p50 dimer interface mutants; one of them revealed a remarkable alteration. One or possibly both its mutations cause a switch into an intertwined dimer, in which the molecular partners exchange nearly half of their fold. In spite of the extensive swapping of secondary structure elements, the topology within each counterpart is preserved, with a very similar overall structure and minimal changes at the interface. Thus intertwining rescues structure and function from a destabilizing mutation. Since the mutants originate from a directed evolution experiment and are functional, the data provide an evolutionary snapshot of how a protein structure can respond to mutations while maintaining a functional molecular architecture.
Snapshot of protein structure evolution reveals conservation of functional dimerization through intertwined folding.,Chirgadze DY, Demydchuk M, Becker M, Moran S, Paoli M Structure. 2004 Aug;12(8):1489-94. PMID:15296742[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Chirgadze DY, Demydchuk M, Becker M, Moran S, Paoli M. Snapshot of protein structure evolution reveals conservation of functional dimerization through intertwined folding. Structure. 2004 Aug;12(8):1489-94. PMID:15296742 doi:10.1016/j.str.2004.06.011
