1my7
From Proteopedia
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| - | [[Image:1my7.gif|left|200px]] | + | [[Image:1my7.gif|left|200px]] |
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| - | '''NF-kappaB p65 subunit dimerization domain homodimer N202R mutation''' | + | {{Structure |
| + | |PDB= 1my7 |SIZE=350|CAPTION= <scene name='initialview01'>1my7</scene>, resolution 1.49Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= RELA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''NF-kappaB p65 subunit dimerization domain homodimer N202R mutation''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MY7 is a [ | + | 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== | ==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:// | + | 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: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:49:44 2008'' |
Revision as of 10:49, 20 March 2008
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| , resolution 1.49Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | RELA (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 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 Thu Mar 20 12:49:44 2008
Categories: Mus musculus | Single protein | Ghosh, G. | Huang, D B. | Hughes, C A. | Huxford, T. | Komives, E A. | Mishler, D. | Phelps, C B. | Reeves, R. | Sengchanthalangsy, L L. | Activator | Beta-sandwich | Beta-sheet | Homodimerdna-binding | Ig | Immunoglobulin | Nuclear protein | Phosphorylation | Transcription regulation
