tailieunhanh - Báo cáo Y học: Structural and biochemical characterization of neuronal calretinin domain I– II (residues 1– 100) Comparison to homologous calbindin D28k domain I–II (residues 1 –93)

Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology, Warsaw, Poland; Department of Biochemistry and Molecular Biology, University of Debrecen, Hungary; 3Department of Inorganic Chemistry, and 4Research Group for Antibiotics, Department of Chemistry, University of Debrecen, Hungary; 5 International Institute of Molecular and Cell Biology, Warsaw, Poland This study characterizes the calcium-bound CR I – II domain (residues 1–100) of rat calretinin (CR). CR, with six EF-hand motifs, is believed to function as a neuronal intracellular calcium-buffer and/or calcium-sensor. . | Eur. J. Biochem. 268 6229-6237 2001 FEBS 2001 Structural and biochemical characterization of neuronal calretinin domain I-II residues 1-100 Comparison to homologous calbindin D28k domain I-II residues 1-93 Mataorzata Palczewska 1 Patrick Groves1 Attila Ambrus2 Aaata Kaleta1. Katalin E Kover3 Gvula Batta4 and Jacek KuZnicki1 5 1 Department of Molecular and Cellular Neurobiology Nencki Institute of Experimental Biology Warsaw Poland 2Department of Biochemistry and Molecular Biology University of Debrecen Hungary 3Department of Inorganic Chemistry and 4Research Group for Antibiotics Department of Chemistry University of Debrecen Hungary 5International Institute of Molecular and Cell Biology Warsaw Poland This study characterizes the calcium-bound CR I-II domain residues 1-100 of rat calretinin CR . CR with six EF-hand motifs is believed to function as a neuronal intracellular calcium-buffer and or calcium-sensor. The secondary structure of CR I-II defined by standard NMR methods on 13C 15N-labeled protein contains four helices and two short interacting segments of extended structure between the calcium-binding loops. The linker between the two helix-loop-helix EF-hand motifs is 12 residues long. Limited trypsinolysis at K60 there are 10 other K R residues in CR I-II confirms that the linker of CR I-II is solvent-exposed and that other potential sites are protected by regular secondary structure. 45Ca-overlay of glutathione S-transferase GST -CR 1-60 and GsT-cR 61-100 fusion proteins confirm that both EF-hands of CR I-II have intrinsic calcium-binding properties. The primary sequence and NMR chemical shifts including calcium-sensitive glycine residues also suggest that both EF-hand loops of CRI-II bind calcium. NMR relaxation analytical ultracentrifugation chemical cross-linking and NMR translation diffusion measurements indicate that CR I-II exists as a monomer. Calb I-II the homologous domain of calbindin D28k has the same EF-hand secondary structures as CR I-II .

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