Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin

Nature Structural Biology

Volumn 10, Issue 3, 2003, Pages 226-231

  Yamauchi, Emiko ^a,b   Nakatsu, Toru ^a   Matsubara, Mamoru ^a,c   Kato, Hiroaki ^a,d   Taniguchi, Hisaaki ^a,b  

^a RIKEN HARIMA INSTITUTE   (Japan)

^b UNIVERSITY OF TOKUSHIMA   (Japan)

^c Nippon Organon KK   (Japan)

^d KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CALMODULIN; CALMODULIN BINDING PROTEIN; MARCKS PROTEIN; PROTEIN KINASE (CALCIUM,CALMODULIN);

ARTICLE; BINDING AFFINITY; BINDING KINETICS; BINDING SITE; CRYSTAL STRUCTURE; CRYSTALLIZATION; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BINDING SITES; CALCIUM; CALMODULIN; CRYSTALLOGRAPHY, X-RAY; HYDROPHOBICITY; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MACROMOLECULAR SUBSTANCES; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PHOSPHOPROTEINS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY;

EID: 0037337760     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb900     Document Type: Article

References (42)

1. Stumpo, D.J., Bock, C.B., Tuttle J.S. & Blackshear, P.J. MARCKS deficiency in mice leads to abnormal brain development and perinatal death. Proc. Natl. Acad. Sci. USA 92, 944-948 (1995).
2. Aderem, A. The MARCKS brothers: a family of protein kinase C substrates. Cell 71, 713-716 (1992).
3. Blackshear, P.J. The MARCKS family of cellular protein kinase C substrates. J. Biol. Chem. 268, 1501-1504 (1993).
4. 2+-calmodulin. FEBS Lett. 421, 203-207 (1998).
5. Wang, J., Arbuzova, A., Hangyas-Mihalyne, G. & McLaughlin, S. The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 276, 5012-5019 (2001).
6. Taniguchi, H. & Manenti, S. Interaction of myristoylated alanine-rich C substrate (MARCKS) with membrane phospholipids. J. Biol. Chem. 268, 9960-9963 (1993).
7. Jin, C.S., Ahn, J.K., Meadows, G.G. & Joe, C.O. Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation. Biochem. Biophys. Res. Commun. 283, 273-277 (2001).
8. Meador, W.E., Means, A.R. & Quiocho, F.A. Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex. Science 257, 1251-1255 (1992).
9. Meador, W.E., Means, A.R. & Quiocho, F.A. Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science 262, 1718-1721 (1993).
10. 2+-calmodulin-dependent kinase kinase. Nat. Struct. Biol. 6, 819-824 (1999).
11. Rhoads, A.R. & Friedberg, F. Sequence motifs for calmodulin recognition. FASEB J. 11, 331-340 (1997).
12. Yap, K.L. et al. Calmodulin target database. J. Struct. Funct. Genomics 1, 8-14 (2000).
13. Qin, Z., Wertz, S.L. Jacob, J., Savino, Y. & Cafiso, D.S. Defining protein-protein interactions using site-directed spin-labeling: the binding of protein kinase C substrates to calmodulin. Biochemistry 35, 13272-13276 (1996).
14. Porumb, T., Crivici, A., Blackshear, P.J. & Ikura, M. Calcium binding and conformational properties of calmodulin complexed with peptides derived from myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein (MRP). Eur. Biophys. J. 23, 239-247 (1997).
15. 1H NMR studies on the structures of peptides derived from the calmodulin-binding domains of inducible and endothelial nitric-oxide synthase in solution and in complex with calmodulin. J. Biol. Chem. 272, 23050-23056 (1997).
16. Ulrich, A. et al. Mapping the interface between calmodulin and MARCKS-related protein by fluorescence spectroscopy. Proc. Natl. Acad. Sci. USA 97, 5191-5196 (2000).
17. Ikura, M. Calcium binding and conformational response in EF-hand proteins. Trends Biochem. Sci. 21, 14-17 (1996).
18. 2+/calmodulin. Nature 410, 1120-1124 (2001).
19. Drum, C.L. et al. Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature 415, 396-402 (2002).
20. 2+ pump. Biochemistry 38, 12320-12332 (1999).
21. Graff, J.M., Young, T.N., Johnson, D. & Blackshear, P.J. Phosphorylation-regulated calmodulin binding to a prominent cellular substrate for protein kinase C. J. Biol. Chem. 264, 21818-21823 (1989).
22. Palmer, R.H. et al. PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. FEBS Lett. 378, 281-285 (1996).
23. Nagumo, H. et al. Rho-associated kinase phosphorylates MARCKS in human neuronal cells. Biochem. Biophys. Res. Commun. 280, 605-609 (2001).
24. McIlroy, B.K., Walters, J.D., Blackshear, P.J. & Johnson, J.D. Phosphorylation-dependent binding of a synthetic MARCKS peptide to calmodulin. J. Biol. Chem. 266, 4959-4964 (1991).
25. Blackshear, P.J., Verghese, G.M., Johnson, J.D., Haupt, D.M. & Stumpo, D.J. Characteristics of the F52 protein, a MARCKS homologue. J. Biol. Chem. 267, 13540-13546 (1992).
26. Matsuoka, Y., Hughes, C.A. & Bennett, V. Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C. J. Biol. Chem. 271, 25157-25166 (1996).
27. Wang, K.L., Khan, M.T. & Roufogalis, B.D. Identification and characterization of a calmodulin-binding domain in Ral-A, a Ras-related GTP-binding protein purified from human erythrocyte membrane. J. Biol. Chem. 272, 16002-16009 (1997).
28. Faux, M.C. & Scott, J.D. Regulation of the AKAP79-protein kinase C interaction by Ca2+-Calmodulin. J. Biol. Chem. 272, 17038-17044 (1997).
29. Pronin, A.N., Satpaev, D.K., Slepak, V.Z. & Benovic, J.L. Regulation of G protein-coupled receptor kinases by calmodulin and localization of the calmodulin binding domain. J. Biol. Chem. 272, 18273-18280 (1997).
30. Bubb, M., Lenox, R.H. & Edison, A.S. Phosphorylation-dependent conformational changes induce a switch in the actin-binding function of MARCKS. J. Biol. Chem. 274, 36472-36478 (1999).
31. Wright, P.E. & Dyson H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293, 321-331 (1999).
32. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
33. Otwinowski, Z. DENZO. in Proceedings of the CCP4 Study Weekend: Data Collection and Processing. (eds. Sawyer, L., Isaacs, N. & Bailey, S.) 56-62 (SERC Daresbury Laboratory, Warrington, UK; 1993).
34. Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
35. Harmat, V. et al. A new potent calmodulin antagonist with arylalkylamine structure: crystallographic, spectroscopic and functional studies. J. Mol. Biol. 297, 747-755 (2000).
36. Roussel, A. & Cambillau, C. TURBO-FRODO Manual (AFMB-CNRS, Marseille; 1996).
37. Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crysallogr. D 50, 760-763 (1994).
38. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
39. Li, Z., Rossi, E.A., Hoheisel, J.D., Kalderon, D. & Rubin, C.S. Generation of a novel A kinase anchor protein and a myristoylated alanine-rich C kinase substrate-like analog from a single gene. J. Biol. Chem. 274, 27191-27200 (1999).
40. Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
41. Merritt, E.A. & Murphy, M.E.P. Raster3D version 2.0: a program for photorealistic molecular graphics. Acta Crystallogr. D 50, 869-873 (1994).
42. Nicholls, A., Sharp, K.A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296 (1991).