View source for 1my7

[[Image:1my7.gif|left|200px]]

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{{STRUCTURE_1my7|  PDB=1my7  |  SCENE=  }} 

'''NF-kappaB p65 subunit dimerization domain homodimer N202R mutation'''


==Overview==
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.

==About this Structure==
1MY7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MY7 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:[http://www.ncbi.nlm.nih.gov/pubmed/12460563 12460563]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Ghosh, G.]]
[[Category: Huang, D B.]]
[[Category: Hughes, C A.]]
[[Category: Huxford, T.]]
[[Category: Komives, E A.]]
[[Category: Mishler, D.]]
[[Category: Phelps, C B.]]
[[Category: Reeves, R.]]
[[Category: Sengchanthalangsy, L L.]]
[[Category: Activator]]
[[Category: Beta-sandwich]]
[[Category: Beta-sheet]]
[[Category: Homodimerdna-binding]]
[[Category: Ig]]
[[Category: Immunoglobulin]]
[[Category: Nuclear protein]]
[[Category: Phosphorylation]]
[[Category: Transcription regulation]]
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