1my5

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[[Image:1my5.gif|left|200px]]
[[Image:1my5.gif|left|200px]]
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{{Structure
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|PDB= 1my5 |SIZE=350|CAPTION= <scene name='initialview01'>1my5</scene>, resolution 1.80&Aring;
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The line below this paragraph, containing "STRUCTURE_1my5", creates the "Structure Box" on the page.
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|GENE= RELA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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{{STRUCTURE_1my5| PDB=1my5 | SCENE= }}
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|RELATEDENTRY=[[1bft|1bft]], [[1my7|1my7]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1my5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1my5 OCA], [http://www.ebi.ac.uk/pdbsum/1my5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1my5 RCSB]</span>
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'''NF-kappaB p65 subunit dimerization domain homodimer'''
'''NF-kappaB p65 subunit dimerization domain homodimer'''
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[[Category: Reeves, R.]]
[[Category: Reeves, R.]]
[[Category: Sengchanthalangsy, L L.]]
[[Category: Sengchanthalangsy, L L.]]
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[[Category: activator]]
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[[Category: Activator]]
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[[Category: beta-sandwich]]
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[[Category: Beta-sandwich]]
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[[Category: beta-sheet]]
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[[Category: Beta-sheet]]
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[[Category: dna-binding]]
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[[Category: Dna-binding]]
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[[Category: homodimer]]
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[[Category: Homodimer]]
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[[Category: ig]]
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[[Category: Ig]]
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[[Category: immunoglobulin]]
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[[Category: Immunoglobulin]]
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[[Category: nuclear protein]]
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[[Category: Nuclear protein]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: transcription regulation]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:51:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:22:46 2008''
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Revision as of 22:51, 2 May 2008

Image:1my5.gif

Template:STRUCTURE 1my5

NF-kappaB p65 subunit dimerization domain homodimer


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

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 Page seeded by OCA on Sat May 3 01:51:41 2008

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OCA

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