Induced fit in RNA-protein recognition.
Two generalizations can be drawn from the recent rapid progress in understanding RNA-protein interactions. First, there is a great diversity of observed protein and RNA structural motifs. Second, formation of almost every RNA-protein complex that has been characterized involves conformational changes in the protein, the RNA, or both. The role of these conformational changes in the biological function of RNA-protein complexes is not at all clear. Whether or not conformational changes are a critical feature of ribonucleoprotein complex assembly or are an unimportant mechanistic detail, the ubiquity of these changes warrants careful consideration of their implications.
Williamson
J R
JR
Department of Molecular Biology and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA. jrwill@scripps.edu
D015394:Molecular Structure; D011485:Protein Binding; D017510:Protein Folding; D012313:RNA / Q000737:chemistry / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000737:chemistry / Q000378:metabolism
D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; D012313:RNA