caa a22 4500 397494394 CHVBK 20180308164517.0 cr unu---uuuuu 161202e199503 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a124745 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a124745 Solution Structure of Cysteine-Rich Domain of Protein Kinase Cα [Elektronische Daten] [Saori Ichikawa, Hideki Hatanaka, Yoriko Takeuchi, Shigeo Ohno, Fuyuhiko Inagaki] The three-dimensional structure of the second cysteine-rich domain of protein kinase Ca (residues 95-159) was determined in aqueous solution by two-dimensional proton nuclear magnetic resonance and simulated annealing based calculations. On the basis of 687 distance constraints derived from assigned nuclear Overhauser effect (NOE) connectivities, a total of 10 converged structures were obtained from 40 runs of calculations. The atomic root-mean-square (RMS) difference about the mean coordinate positions (excluding residues 1-7,16-, 30-34, and 55-65) is 0.55 Â for backbone atoms (N, Cα C′) and 1.07 Â for all non-hydrogen atoms. The molecular scaffold is maintained by triple-stranded and double-stranded twisted β-sheets packed against an α-helix and two independent zincs are coordinated by His8, Cys38, Cys41, Cys57 and Cys21, Cys24, His46, Cys49, respectively. It should be noted that the metal ligands from the two sites are interleaved and this is thought to be a new structural motif of a zinc finger domain. Based on the resultant structure, we propose an interaction site of the cysteine-rich domain of protein kinase C with diacylglyc-erols and phorbol esters. © 1995 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence cysteine-rich domain nationallicence distance geometry nationallicence protein kinase C nationallicence three-dimensional protein structure nationallicence zinc coordination site nationallicence Ichikawa Saori Department of Molecular Physiology, The Tokyo Metropolitan Institute of Medical Science 3-18-22 Honkomagome, Bunkyo-ku, Tokyo 113 aut Hatanaka Hideki Department of Molecular Physiology, The Tokyo Metropolitan Institute of Medical Science 3-18-22 Honkomagome, Bunkyo-ku, Tokyo 113 aut Takeuchi Yoriko Department of Molecular Biology, Yokohama City University School of Medicine 3-9 Fuku-ura, Kanazawa-ku, Yokohama 236 aut Ohno Shigeo Department of Molecular Biology, Yokohama City University School of Medicine 3-9 Fuku-ura, Kanazawa-ku, Yokohama 236 aut Inagaki Fuyuhiko Department of Molecular Biology, Yokohama City University School of Medicine 3-9 Fuku-ura, Kanazawa-ku, Yokohama 236 aut The Journal of Biochemistry Oxford University Press 117/3(1995-03), 566-574 0021-924X 117:3<566 1995 117 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a124745 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a124745 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ichikawa Saori Department of Molecular Physiology, The Tokyo Metropolitan Institute of Medical Science 3-18-22 Honkomagome, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Hatanaka Hideki Department of Molecular Physiology, The Tokyo Metropolitan Institute of Medical Science 3-18-22 Honkomagome, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Takeuchi Yoriko Department of Molecular Biology, Yokohama City University School of Medicine 3-9 Fuku-ura, Kanazawa-ku, Yokohama 236 aut NATIONALLICENCE 700 1- Ohno Shigeo Department of Molecular Biology, Yokohama City University School of Medicine 3-9 Fuku-ura, Kanazawa-ku, Yokohama 236 aut NATIONALLICENCE 700 1- Inagaki Fuyuhiko Department of Molecular Biology, Yokohama City University School of Medicine 3-9 Fuku-ura, Kanazawa-ku, Yokohama 236 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 117/3(1995-03), 566-574 0021-924X 117:3<566 1995 117 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford