1my5: Difference between revisions

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[[Image:1my5.gif|left|200px]]
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[[Image:1my5.png|left|200px]]


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{{STRUCTURE_1my5|  PDB=1my5  |  SCENE=  }}  
{{STRUCTURE_1my5|  PDB=1my5  |  SCENE=  }}  


'''NF-kappaB p65 subunit dimerization domain homodimer'''
===NF-kappaB p65 subunit dimerization domain homodimer===




==Overview==
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IkappaBalpha inhibits transcription factor NF-kappaB activity by specific binding to NF-kappaB heterodimers composed of p65 and p50 subunits. It binds with slightly lower affinity to p65 homodimers and with significantly lower affinity to homodimers of p50. We have employed a structure-based mutagenesis approach coupled with protein-protein interaction assays to determine the source of this dimer selectivity exhibited by IkappaBalpha. Mutation of amino acid residues in IkappaBalpha that contact NF-kappaB only marginally affects complex binding affinity, indicating a lack of hot spots in NF-kappaB/IkappaBalpha complex formation. Conversion of the weak binding NF-kappaB p50 homodimer into a high affinity binding partner of IkappaBalpha requires transfer of both the NLS polypeptide and amino acid residues Asn202 and Ser203 from the NF-kappaB p65 subunit. Involvement of Asn202 and Ser203 in complex formation is surprising as these amino acid residues occupy solvent exposed positions at a distance of 20A from IkappaBalpha in the crystal structures. However, the same amino acid residue positions have been genetically isolated as determinants of binding specificity in a homologous system in Drosophila. X-ray crystallographic and solvent accessibility experiments suggest that these solvent-exposed amino acid residues contribute to NF-kappaB/IkappaBalpha complex formation by modulating the NF-kappaB p65 subunit NLS polypeptide.
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{{ABSTRACT_PUBMED_12460563}}


==About this Structure==
==About this Structure==
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[[Category: Phosphorylation]]
[[Category: Phosphorylation]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:51:41 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:51:27 2008''

Revision as of 04:51, 29 July 2008

File:1my5.png

Template:STRUCTURE 1my5

NF-kappaB p65 subunit dimerization domain homodimer

Template:ABSTRACT PUBMED 12460563

About this Structure

1MY5 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Solvent exposed non-contacting amino acids play a critical role in NF-kappaB/IkappaBalpha complex formation., Huxford T, Mishler D, Phelps CB, Huang DB, Sengchanthalangsy LL, Reeves R, Hughes CA, Komives EA, Ghosh G, J Mol Biol. 2002 Dec 6;324(4):587-97. PMID:12460563

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