1lui
|
NMR Structures of Itk SH2 domain, Pro287cis isoform, ensemble of 20 low energy structures
OverviewOverview
Interleukin-2 tyrosine kinase (Itk) is a T cell-specific kinase required, for a proper immune response following T cell receptor engagement. In, addition to the kinase domain, Itk is composed of several noncatalytic, regulatory domains, including a Src homology 2 (SH2) domain that contains, a conformationally heterogeneous Pro residue. Cis-trans isomerization of a, single prolyl imide bond within the SH2 domain mediates conformer-specific, ligand recognition that may have functional implications in T cell, signaling. To better understand the mechanism by which a proline switch, regulates ligand binding, we have used NMR spectroscopy to determine two, structures of Itk SH2 corresponding to the cis and trans imide, bond-containing conformers. The structures indicate that the heterogeneous, Pro residue acts as a hinge that modulates ligand recognition by, controlling the relative orientation of protein-binding surfaces.
About this StructureAbout this Structure
1LUI is a Single protein structure of sequence from Mus musculus with ACE and NH2 as ligands. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
ReferenceReference
Structural characterization of a proline-driven conformational switch within the Itk SH2 domain., Mallis RJ, Brazin KN, Fulton DB, Andreotti AH, Nat Struct Biol. 2002 Dec;9(12):900-5. PMID:12402030
Page seeded by OCA on Tue Nov 20 20:53:56 2007