2odg
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The barrier-to-autointegration factor BAF binds to the LEM domain | + | The barrier-to-autointegration factor BAF binds to the LEM domain (Em(LEM)) of the nuclear envelope protein emerin and plays an essential role in the nuclear architecture of metazoan cells. In addition, the BAF(2) dimer bridges and compacts double-stranded DNA nonspecifically via two symmetry-related DNA binding sites. In this article we present biophysical and structural studies on a complex of BAF(2) and Em(LEM). Light scattering, analytical ultracentrifugation, and NMR indicate a stoichiometry of one molecule of Em(LEM) bound per BAF(2) dimer. The equilibrium dissociation constant (K(d)) for the interaction of the BAF(2) dimer and Em(LEM), determined by isothermal titration calorimetry, is 0.59 +/- 0.03 microm. Z-exchange spectroscopy between corresponding cross-peaks of the magnetically non-equivalent subunits of the BAF(2) dimer in the complex yields a dissociation rate constant of 78 +/- 2s(-1). The solution NMR structure of the BAF(2)-Em(LEM) complex reveals that the LEM and DNA binding sites on BAF(2) are non-overlapping and that both subunits of the BAF(2) dimer contribute approximately equally to the Em(LEM) binding site. The relevance of the implications of the structural and biophysical data on the complex in the context of the interaction between the BAF(2) dimer and Em(LEM) at the nuclear envelope is discussed. |
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| + | ==Disease== | ||
| + | Known diseases associated with this structure: Emery-Dreifuss muscular dystrophy OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300384 300384]], Epilepsy, myoclonic, benign adult familial OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601068 601068]] | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Solution NMR | + | Solution NMR structure of the barrier-to-autointegration factor-Emerin complex., Cai M, Huang Y, Suh JY, Louis JM, Ghirlando R, Craigie R, Clore GM, J Biol Chem. 2007 May 11;282(19):14525-35. Epub 2007 Mar 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17355960 17355960] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Cai, M.]] | [[Category: Cai, M.]] | ||
| - | [[Category: Clore, G | + | [[Category: Clore, G M.]] |
[[Category: inner nuclear membrane protein]] | [[Category: inner nuclear membrane protein]] | ||
[[Category: lem-domain baf multidimensional nmr dipolar couplings]] | [[Category: lem-domain baf multidimensional nmr dipolar couplings]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:17:10 2008'' |
Revision as of 16:17, 21 February 2008
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Complex of barrier-to-autointegration factor and LEM-domain of emerin
Contents |
Overview
The barrier-to-autointegration factor BAF binds to the LEM domain (Em(LEM)) of the nuclear envelope protein emerin and plays an essential role in the nuclear architecture of metazoan cells. In addition, the BAF(2) dimer bridges and compacts double-stranded DNA nonspecifically via two symmetry-related DNA binding sites. In this article we present biophysical and structural studies on a complex of BAF(2) and Em(LEM). Light scattering, analytical ultracentrifugation, and NMR indicate a stoichiometry of one molecule of Em(LEM) bound per BAF(2) dimer. The equilibrium dissociation constant (K(d)) for the interaction of the BAF(2) dimer and Em(LEM), determined by isothermal titration calorimetry, is 0.59 +/- 0.03 microm. Z-exchange spectroscopy between corresponding cross-peaks of the magnetically non-equivalent subunits of the BAF(2) dimer in the complex yields a dissociation rate constant of 78 +/- 2s(-1). The solution NMR structure of the BAF(2)-Em(LEM) complex reveals that the LEM and DNA binding sites on BAF(2) are non-overlapping and that both subunits of the BAF(2) dimer contribute approximately equally to the Em(LEM) binding site. The relevance of the implications of the structural and biophysical data on the complex in the context of the interaction between the BAF(2) dimer and Em(LEM) at the nuclear envelope is discussed.
Disease
Known diseases associated with this structure: Emery-Dreifuss muscular dystrophy OMIM:[300384], Epilepsy, myoclonic, benign adult familial OMIM:[601068]
About this Structure
2ODG is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution NMR structure of the barrier-to-autointegration factor-Emerin complex., Cai M, Huang Y, Suh JY, Louis JM, Ghirlando R, Craigie R, Clore GM, J Biol Chem. 2007 May 11;282(19):14525-35. Epub 2007 Mar 13. PMID:17355960
Page seeded by OCA on Thu Feb 21 18:17:10 2008
