title: Crystal and solution structures disclose a putative transient state of mitogen-activated protein kinase kinase 4.
abstract: Mitogen-activated protein kinase kinase 4 (MAP2K4) plays a crucial role in the stress-activated signal cascade and is enzymatically regulated by ligand or substrate binding, and/or post-translational modification. Crystal structures combined with small-angle X-ray scattering experiments revealed that the apo form of non-phosphorylated MAP2K4 (npMAP2K4) exists in a transient state which has a longer conformation compared with the typical kinase folding. Upon ATP-binding, the transient conformation adopted the configuration of typical kinase folding. In the absence of ATP-binding, the transient state of apo npMAP2K4 may shift to a state of aggregation via non-particular hydrophobic interactions as a result of the exposed hydrophobic residues.
authors: Rigaku Corporation, Akishima, Tokyo 196-8666, Japan. t-matumo@rigaku.co.jp
authors: Takashi
authors: T
authors: Matsumoto
authors: Takayoshi
authors: T
authors: Kinoshita
authors: Yasuyuki
authors: Y
authors: Kirii
authors: Toshiji
authors: T
authors: Tada
authors: Akihito
authors: A
authors: Yamano
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry; D018360:Crystallography, X-Ray; D006801:Humans; D048670:MAP Kinase Kinase 4 / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D012542:Scattering, Radiation; D053838:Scattering, Small Angle; D014961:X-Ray Diffraction
chemical_list: D000255:Adenosine Triphosphate; D048670:MAP Kinase Kinase 4