2ODC

LEM-domain of the nuclear envelope protein emerin

Summary for 2ODC

• Entry DOI: 10.2210/pdb2odc/pdb
• Related: 2ODG
• Descriptor: Emerin (1 entity in total)
• Functional Keywords: inner nuclear membrane protein, lem-domain multidimensional nmr dipolar couplings, membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus inner membrane; Single-pass membrane protein; Nucleoplasmic side: P50402
• Total number of polymer chains: 1
• Total formula weight: 5720.40

Authors

Clore, G.M.,Cai, M. (deposition date: 2006-12-22, release date: 2007-03-13, Last modification date: 2023-12-27)

Primary citation

Cai, M.,Huang, Y.,Suh, J.Y.,Louis, J.M.,Ghirlando, R.,Craigie, R.,Clore, G.M.
Solution NMR Structure of the Barrier-to-Autointegration Factor-Emerin Complex.
J.Biol.Chem., 282:14525-14535, 2007

PubMed Abstract: 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.

PubMed: 17355960
DOI: 10.1074/jbc.M700576200

Experimental method

SOLUTION NMR