关键词： FMN G-protein coupled receptor GDP GPCR GTP HSQC Human Raf-1 kinase inhibitor protein (hRKIP) Ligand-binding pocket MAPK Model-free analysis NF-κB NMR NOE NOESY PE Protein dynamics R(1) R(2) R(ex) RKIP RMSD Raf-1 kinase inhibitor protein S(2) Solution structure conformational exchange rate flavin mononucleotide guanosine di-phosphate guanosine tri-phosphate heteronuclear singular quantum correlation longitudinal relaxation rate mitogen-activated protein kinase nuclear factor-kappa B nuclear overhauser effect nuclear overhauser enhancement spectroscopy o-phosphorylethanolamine order parameters root-mean-square deviation transverse relaxation rate

Mesh ： Amino Acid Sequence Binding Sites Computer Simulation Humans Models, Chemical Models, Molecular Molecular Sequence Data Phosphatidylethanolamine Binding Protein / chemistry ultrastructure Protein Binding Protein Conformation Proto-Oncogene Proteins c-raf / chemistry ultrastructure

来  源：   DOI：10.1016/j.bbrc.2013.07.039   PDF(Sci-hub)

Abstract：
Human Raf-1 kinase inhibitor protein (hRKIP) is a small multi-functional protein of 187 residues. It contains a conserved pocket, which binds a wide range of ligands from various small molecules to distinct proteins. To provide a structural basis for the ligand diversity of RKIP, we herein determined the solution structure of hRKIP, and analyzed its structural dynamics. In solution, hRKIP mainly comprises two antiparallel β sheets, two α helices and two 3₁₀ helices. NMR dynamic analysis reveals that the overall structure of hRKIP is rigid, but its C-terminal helix which is close to the ligand-binding site is mobile. In addition, residues around the ligand-binding pocket exhibit significant conformational exchange on the μs-ms timescale. Conformational flexibility may allow the ligand-binding pocket and the C-terminal helix to adopt various conformations to interact with different substrates. This work may shed light on the underlying molecular mechanisms of how hRKIP recognizes and binds diverse substrate ligands.
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