1u3y
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= Nfkb1, 18033 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= Nfkb1, 18033 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1u36|1U36]], [[1u3j|1U3J]], [[1u3z|1U3Z]], [[1u41|1U41]], [[1u42|1U42]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u3y OCA], [http://www.ebi.ac.uk/pdbsum/1u3y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u3y RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Moran, S.]] | [[Category: Moran, S.]] | ||
[[Category: Paoli, M.]] | [[Category: Paoli, M.]] | ||
| - | [[Category: | + | [[Category: dimerization domain]] |
| + | [[Category: intertwined folding]] | ||
| + | [[Category: nf-kb]] | ||
| + | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:05:05 2008'' |
Revision as of 21:05, 30 March 2008
| |||||||
| , resolution 1.901Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | Nfkb1, 18033 (Mus musculus) | ||||||
| Related: | 1U36, 1U3J, 1U3Z, 1U41, 1U42
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal stucture of ILAC mutant of dimerisation domain of NF-kB p50 transcription factor
Overview
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.
About this Structure
1U3Y is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
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