1u3y

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[[Image:1u3y.jpg|left|200px]]
[[Image:1u3y.jpg|left|200px]]
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{{Structure
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|PDB= 1u3y |SIZE=350|CAPTION= <scene name='initialview01'>1u3y</scene>, resolution 1.901&Aring;
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The line below this paragraph, containing "STRUCTURE_1u3y", creates the "Structure Box" on the page.
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|SITE=
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|GENE= Nfkb1, 18033 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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|DOMAIN=
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{{STRUCTURE_1u3y| PDB=1u3y | SCENE= }}
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|RELATEDENTRY=[[1u36|1U36]], [[1u3j|1U3J]], [[1u3z|1U3Z]], [[1u41|1U41]], [[1u42|1U42]]
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|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>
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'''Crystal stucture of ILAC mutant of dimerisation domain of NF-kB p50 transcription factor'''
'''Crystal stucture of ILAC mutant of dimerisation domain of NF-kB p50 transcription factor'''
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[[Category: Moran, S.]]
[[Category: Moran, S.]]
[[Category: Paoli, M.]]
[[Category: Paoli, M.]]
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[[Category: dimerization domain]]
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[[Category: Dimerization domain]]
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[[Category: intertwined folding]]
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[[Category: Intertwined folding]]
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[[Category: nf-kb]]
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[[Category: Nf-kb]]
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[[Category: transcription factor]]
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[[Category: Transcription factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:05:05 2008''
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Revision as of 07:44, 3 May 2008

Template:STRUCTURE 1u3y

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 Page seeded by OCA on Sat May 3 10:44:05 2008

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