Domain swapping and different oligomeric states for the complex between calmodulin and the calmodulin-binding domain of calcineurin A

PLoS ONE

Volumn 4, Issue 4, 2009, Pages

  Majava, Viivi ^a   Kursula, Petri ^a  

^a UNIVERSITY OF OULU   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

CALCINEURIN; CALCINEURIN A; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; CALMODULIN; MONOMER; UNCLASSIFIED DRUG; PEPTIDE FRAGMENT;

ARTICLE; BINDING SITE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; ENERGY TRANSFER; GEL PERMEATION CHROMATOGRAPHY; HUMAN; ISOTHERMAL TITRATION CALORIMETRY; LIGAND BINDING; MOLECULAR SIZE; NONHUMAN; OLIGOMERIZATION; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; X RAY CRYSTALLOGRAPHY; ANIMAL; CALORIMETRY; GEL CHROMATOGRAPHY; METABOLISM; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; SMALL ANGLE SCATTERING; SOLUTION AND SOLUBILITY; X RAY DIFFRACTION;

ANIMALS; BINDING SITES; CALCINEURIN; CALMODULIN; CALORIMETRY; CHROMATOGRAPHY, GEL; HUMANS; PEPTIDE FRAGMENTS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; SCATTERING, SMALL ANGLE; SOLUTIONS; X-RAY DIFFRACTION;

EID: 65549147594     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0005402     Document Type: Article

References (37)

1. Hoeflich KP, Ikura M (2002) Calmodulin in action: diversity in target recognition and activation mechanisms. Cell 108: 739-742.
2. Heidorn DB, Seeger PA, Rokop SE, Blumenthal DK, Means AR, et al. (1989) Changes in the structure of calmodulin induced by a peptide based on the calmodulin-binding domain of myosin light chain kinase. Biochemistry 28: 6757-6764.
3. Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, et al. (1992) Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256: 632-638.
4. Meador WE, Means AR, Quiocho FA (1992) Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. Science 257: 1251-1255.
5. Aoyagi M, Arvai AS, Tainer JA, Getzoff ED (2003) Structural basis for endothelial nitric oxide synthase binding to calmodulin. EMBO J 22: 766-775.
6. Clapperton JA, Martin SR, Smerdon SJ, Gamblin SJ, Bayley PM (2002) Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I: studies of the kinase activation mechanism. Biochemistry 41: 14669-14679.
7. Hayashi N, Izumi Y, Titani K, Matsushima N (2000) The binding of myristoylated N-terminal nonapeptide from neuro-specific protein CAP-23/ NAP-22 to calmodulin does not induce the globular structure observed for the calmodulin-nonmyristylated peptide complex. Protein Sci 9: 1905-1913.
8. Izumi Y, Watanabe H, Watanabe N, Aoyama A, Jinbo Y, et al. (2008) Solution X-ray scattering reveals a novel structure of calmodulin complexed with a binding domain peptide from the HIV-1 matrix protein p17. Biochemistry 47: 7158-7166.
9. Majava V, Petoukhov MV, Hayashi N, Pirila P, Svergun DI, et al. (2008) Interaction between the C-terminal region of human myelin basic protein and calmodulin: analysis of complex formation and solution structure. BMC Struct Biol 8: 10.
10. Matsubara M, Nakatsu T, Kato H, Taniguchi H (2004) Crystal structure of a myristoylated CAP-23/NAP-22 N-terminal domain complexed with Ca2+/ calmodulin. EMBO J 23: 712-718.
11. Yamniuk AP, Vogel HJ (2004) Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides. Mol Biotechnol 27: 33-57.
12. Ye Q, Li X, Wong A, Wei Q, Jia Z (2006) Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode. Biochemistry 45: 738-745.
13. Ye Q, Wang H, Zheng J, Wei Q, Jia Z (2008) The complex structure of calmodulin bound to a calcineurin peptide. Proteins 73: 19-27.
14. Zhang Y, Tan H, Jia Z, Chen G (2008) Ligand-induced dimer formation of calmodulin. J Mol Recognit 21: 267-274.
15. Noguchi M, Izumi Y, Yoshino H (2004) Target recognition by calmodulin: the role of acid region contiguous to the calmodulin-binding domain of calcineurin A. FEBS Lett 573: 121-126.
16. Yap KL, Kim J, Truong K, Sherman M, Yuan T, et al. (2000) Calmodulin target database. J Struct Funct Genomics 1: 8-14.
17. Carruthers NJ, Stemmer PM (2008) Methionine oxidation in the calmodulin-binding domain of calcineurin disrupts calmodulin binding and calcineurin activation. Biochemistry 47: 3085-3095.
18. Hayward S, Lee RA (2002) Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50. J Mol Graph Model 21: 181-183.
19. Brokx RD, Lopez MM, Vogel HJ, Makhatadze GI (2001) Energetics of target peptide binding by calmodulin reveals different modes of binding. J Biol Chem 276: 14083-14091.
20. Hayashi N, Matsubara M, Takasaki A, Titani K, Taniguchi H (1998) An expression system of rat calmodulin using T7 phage promoter in Escherichia coli. Protein Expr Purif 12: 25-28.
21. Kursula P, Majava V (2007) A structural insight into lead neurotoxicity and calmodulin activation by heavy metals. Acta Crystallogr Sect F Struct Biol Cryst Commun 63: 653-656.
22. Ursby T, Mammeb CB, Cerenius Y, Svensson C, Sommarin B, et al. (2004) The new macromolecular crystallography stations at MAX-lab: The MAD station. AIP Conference Proceedings 705: 1241-1246.
23. Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Cryst 26: 795-800.
24. Kursula P (2004) XDSi - a graphical interface for the data processing program XDS. J Appl Cryst 37: 347-348.
25. Vagin A, Teplyakov A (1997) MOLREP: an automated program for molecular replacement. J Appl Cryst 30: 1022-1025.
26. Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53: 240-255.
27. Painter J, Merritt EA (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr D Biol Crystallogr 62: 439-450.
28. Winn MD, Isupov MN, Murshudov GN (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr D Biol Crystallogr 57: 122-133.
29. Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
30. Konarev PV, Petoukhov MV, Volkov VV, Svergun DI (2006) ATSAS 2.1, a program package for small-angle scattering data analysis. J Appl Cryst 39: 277-286.
31. Majava V, Loytynoja N, Chen WQ, Lubec G, Kursula P (2008) Crystal and solution structure, stability and post-translational modifications of collapsin response mediator protein 2. FEBS J 275: 4583-4596.
32. Konarev PV, Volkov VV, Sokolova AV, Koch MHJ, Svergun DI (2003) PRIMUS - a Windows-PC based system for small-angle scattering data analysis. J Appl Crystallogr 36: 1277-1282.
33. Svergun DI (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Crystallogr 25: 495-503.
34. Svergun DI (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys J 76: 2879-2886.
35. Volkov VV, Svergun DI (2003) Uniqueness of ab initio shape determination in small angle scattering. J Appl Crystallogr 36: 860-864.
36. Kozin MB, Svergun DI (2001) Automated matching of high- and low-resolution structural models. J Appl Crystallogr 34: 33-41.
37. Svergun DI, Barberato C, Koch MHJ (1995) CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J Appl Crystallogr 28: 768-773.