2odc: Difference between revisions
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New page: left|200px<br /> <applet load="2odc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2odc" /> '''LEM-domain of the nuclear envelope protein ... |
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[[Image:2odc.gif|left|200px]]<br /> | [[Image:2odc.gif|left|200px]]<br /><applet load="2odc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''LEM-domain of the nuclear envelope protein emerin'''<br /> | '''LEM-domain of the nuclear envelope protein emerin'''<br /> | ||
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==Overview== | ==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 mum. 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. | 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 mum. 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. | ||
==About this Structure== | ==About this Structure== | ||
2ODC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 2ODC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ODC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: lem-domain multidimensional nmr dipolar couplings]] | [[Category: lem-domain multidimensional nmr dipolar couplings]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:09:33 2008'' | ||
