An antiparallel four-helix bundle orients the high-affinity RNA binding sites in hnRNP C: a mechanism for RNA chaperonin activity

Previous studies have shown that the C protein of 40 S hnRNP complexes contains a leucine-zipper domain, residues 180-207, and that a 40 residue highly basic domain, immediately preceding the zipper, is responsible for almost all of the free energy of RNA binding to C protein. Because this domain ar...

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Veröffentlicht in:	Journal of molecular biology 2001-01, Vol.305 (4), p.817-828
Hauptverfasser:	Shahied, Lillian, Braswell, Emory H, LeStourgeon, Wallace M, Krezel, Andrzej M
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Binding Sites bZIP protein Chromatography, Gel Heterogeneous-Nuclear Ribonucleoprotein Group C Heterogeneous-Nuclear Ribonucleoproteins hnRNP hnRNPc protein Humans leucine zipper Leucine Zippers Models, Molecular Molecular Chaperones - chemistry Molecular Chaperones - metabolism Molecular Sequence Data NMR Nuclear Magnetic Resonance, Biomolecular Protein Binding Protein Structure, Quaternary Protein Structure, Tertiary ribonucleoprotein Ribonucleoproteins - chemistry Ribonucleoproteins - metabolism RNA - chemistry RNA - genetics RNA - metabolism RNA binding RNA-Binding Proteins - chemistry RNA-Binding Proteins - metabolism Sequence Alignment Thermodynamics
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