1LUK

NMR Structure of the Itk SH2 domain, Pro287cis, Energy minimized average structure

Summary for 1LUK

• Entry DOI: 10.2210/pdb1luk/pdb
• Related: 1LUI 1LUM 1LUN
• NMR Information: BMRB: 5461
• Descriptor: Tyrosine-protein kinase ITK/TSK (1 entity in total)
• Functional Keywords: cis/trans isomerization, interleukin-2 tyrosine kinase, itk, t-cell specific kinase, tsk, src homology 2, sh2, proline, transferase
• Biological source: Mus musculus (house mouse)
• Cellular location: Cell membrane: Q03526
• Total number of polymer chains: 1
• Total formula weight: 12558.25

Authors

Mallis, R.J.,Brazin, K.N.,Fulton, B.F.,Andreotti, A.H. (deposition date: 2002-05-22, release date: 2002-11-27, Last modification date: 2024-10-30)

Primary citation

Mallis, R.J.,Brazin, K.N.,Fulton, D.B.,Andreotti, A.H.
Structural characterization of a proline-driven conformational switch within the Itk SH2 domain
Nat.Struct.Biol., 9:900-905, 2002

PubMed Abstract: 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.

PubMed: 12402030
DOI: 10.1038/nsb864

Experimental method

SOLUTION NMR