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The hnRNP K homology (KH) domain was first identified in the protein human heterogeneous nuclear ribonucleoprotein K (hnRNP K) 14 years ago. Since then, KH domains have been identified as nucleic acid recognition motifs in proteins that perform a wide range of cellular functions. | REVIEW ARTICLE Structure and function of KH domains Roberto Valverde1 Laura Edwards2 and Lynne Regan1 3 1 Department of Molecular Biophysics Biochemistry Yale University New Haven CT USA 2 Department of Molecular and Cellular DevelopmentalBiology Yale University New Haven CT USA 3 Department of Chemistry Yale University New Haven CT USA Keywords fragile X mental retardation interaction motif KH domains K homology domain noncrystallographic symmetry protein motif RNA-binding RNA-binding protein RNA-recognition solvent accessibility Correspondence L. Regan Yale University 266 Whitney Avenue New Haven CT 06520 USA Fax 1 203 432 3104 Tel 1 203 432 9843 E-mail lynne.regan@yale.edu Received 3 January 2008 revised 18 February 2008 accepted 14 March 2008 doi 10.1111 j.1742-4658.2008.06411.x The hnRNP K homology KH domain was first identified in the protein human heterogeneous nuclear ribonucleoprotein K hnRNP K 14 years ago. Since then KH domains have been identified as nucleic acid recognition motifs in proteins that perform a wide range of cellular functions. KH domains bind RNA or ssDNA and are found in proteins associated with transcriptional and translational regulation along with other cellular processes. Several diseases e.g. fragile X mental retardation syndrome and paraneoplastic disease are associated with the loss of function of a particular KH domain. Here we discuss the progress made towards understanding both general and specific features of the molecular recognition of nucleic acids by KH domains. The typical binding surface of KH domains is a cleft that is versatile but that can typically accommodate only four unpaired bases. Van der Waals forces and hydrophobic interactions and to a lesser extent electrostatic interactions contribute to the nucleic acid binding affinity. Augmented KH domains or multiple copies of KH domains within a protein are two strategies that are used to achieve greater affinity and specificity of nucleic acid binding. Isolated KH .
