1u3j

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{{STRUCTURE_1u3j| PDB=1u3j | SCENE= }}
{{STRUCTURE_1u3j| PDB=1u3j | SCENE= }}
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'''Crystal stucture of MLAV mutant of dimerisation domain of NF-kB p50 transcription factor'''
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===Crystal stucture of MLAV mutant of dimerisation domain of NF-kB p50 transcription factor===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15296742 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15296742}}
==About this Structure==
==About this Structure==
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[[Category: Nf-kb]]
[[Category: Nf-kb]]
[[Category: Transcription factor]]
[[Category: Transcription factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:43:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:56:01 2008''

Revision as of 23:56, 27 July 2008

Image:1u3j.png

Template:STRUCTURE 1u3j

Crystal stucture of MLAV mutant of dimerisation domain of NF-kB p50 transcription factor

Template:ABSTRACT PUBMED 15296742

About this Structure

1U3J 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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