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Solution structure of human Ca2+-bound S100A12

  • NMR Structure Note
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References

  • Cornilescu G, Delaglio F, Bax A (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13(3):289–302

    Article  Google Scholar 

  • Dell’Angelica EC, Schleicher CH, Santome JA (1994) Primary structure and binding properties of calgranulin C, a novel S100-like calcium-binding protein from pig granulocytes. J Biol Chem 269(46):28929–28936

    Google Scholar 

  • Donato R (2001) S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles. Int J Biochem Cell Biol 33(7):637–668

    Article  Google Scholar 

  • Eckert RL, Broome AM, Ruse M, Robinson N, Ryan D, Lee K (2004) S100 proteins in the epidermis. J Invest Dermatol 123(1):23–33

    Article  Google Scholar 

  • Filipek A, Jastrzebska B, Nowotny M, Kuznicki J (2002) CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family. J Biol Chem 277(32):28848–28852

    Article  Google Scholar 

  • Foell D, Frosch M, Sorg C, Roth J (2004) Phagocyte-specific calcium-binding S100 proteins as clinical laboratory markers of inflammation. Clinica Chimica Acta 344(1–2):37–51

    Article  Google Scholar 

  • Foell D, Wittkowski H, Vogl T, Roth J (2007) S100 proteins expressed in phagocytes: a novel group of damage-associated molecular pattern molecules. J Leukoc Biol 81(1):28–37

    Article  Google Scholar 

  • Guignard F, Mauel J, Markert M (1995) Identification and characterization of a novel human neutrophil protein related to the S100 family. Biochem J 309(Pt 2):395–401

    Google Scholar 

  • Hofmann MA, Drury S, Fu C, Qu W, Taguchi A, Lu Y, Avila C, Kambham N, Bierhaus A, Nawroth P, Neurath MF, Slattery T, Beach D, McClary J, Nagashima M, Morser J, Stern D, Schmidt AM (1999) RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides. Cell 97(7):889–901

    Article  Google Scholar 

  • Koradi R, Billeter M, Wuthrich K (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Grap 14(1):51–55, 29–32

    Google Scholar 

  • Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8(4):477–486

    Article  Google Scholar 

  • Moroz OV, Antson AA, Murshudov GN, Maitland NJ, Dodson GG, Wilson KS, Skibshoj I, Lukanidin EM, Bronstein IB (2001) The three-dimensional structure of human S100A12. Acta Crystallogr Sect D: Biol Crystallogr 57(Pt 1):20–29

    Article  Google Scholar 

  • Moroz OV, Antson AA, Dodson EJ, Burrell HJ, Grist SJ, Lloyd RM, Maitland NJ, Dodson GG, Wilson KS, Lukanidin E, Bronstein IB (2002) The structure of S100A12 in a hexameric form and its proposed role in receptor signalling. Acta Crystallogr Sect D: Biol Crystallogr 58(Pt 3):407–413

    Article  Google Scholar 

  • Moroz OV, Antson AA, Grist SJ, Maitland NJ, Dodson GG, Wilson KS, Lukanidin E, Bronstein IB (2003) Structure of the human S100A12-copper complex: implications for host-parasite defence. Acta Crystallogr Sect D: Biol Crystallogr 59(Pt 5):859–867

    Article  Google Scholar 

  • Moroz OV, Blagova EV, Wilkinson AJ, Wilson KS, Bronstein IB (2009a) The crystal structures of human S100A12 in apo form and in complex with zinc: new insights into S100A12 oligomerisation. J Mol Biol 391(3):536–551

    Article  Google Scholar 

  • Moroz OV, Burkitt W, Wittkowski H, He W, Ianoul A, Novitskaya V, Xie J, Polyakova O, Lednev IK, Shekhtman A, Derrick PJ, Bjoerk P, Foell D, Bronstein IB (2009b) Both Ca2+ and Zn2+ are essential for S100A12 protein oligomerization and function. BMC Biochem 10:11

    Article  Google Scholar 

  • Potts BC, Smith J, Akke M, Macke TJ, Okazaki K, Hidaka H, Case DA, Chazin WJ (1995) The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins. Nat Struct Biol 2(9):790–796

    Article  Google Scholar 

  • Rieping W, Habeck M, Bardiaux B, Bernard A, Malliavin TE, Nilges M (2007) ARIA2: automated NOE assignment and data integration in NMR structure calculation. Bioinformatics 23(3):381–382

    Article  Google Scholar 

  • Scheiber-Camoretti R, Mehrotra A, Yan L, Raman J, Beshai JF, Hofmann Bowman MA (2013) Elevated S100A12 and sRAGE are associated with increased length of hospitalization after non-urgent coronary artery bypass grafting surgery. Am J Cardiovas Dis 3(2):85–90

    Google Scholar 

  • Smith SP, Shaw GS (1998) A change-in-hand mechanism for S100 signalling. Biochemistry and cell biology. Biochimie et biologie cellulaire 76(2–3):324–333

    Article  Google Scholar 

  • Wishart DS, Sykes BD (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4(2):171–180

    Article  Google Scholar 

  • Xie J, Burz DS, He W, Bronstein IB, Lednev I, Shekhtman A (2007) Hexameric calgranulin C (S100A12) binds to the receptor for advanced glycated end products (RAGE) using symmetric hydrophobic target-binding patches. J Biol Chem 282(6):4218–4231

    Article  Google Scholar 

  • Yap KL, Ames JB, Swindells MB, Ikura M (2002) Vector geometry mapping. A method to characterize the conformation of helix-loop-helix calcium-binding proteins. Methods Mol Biol 173:317–324

    Google Scholar 

Download references

Acknowledgments

This work was supported by grants from the National Science Council of the Republic of China (NSC 102-2731-M-007-002-MY2 to K.W. Hung and NSC 100-2113-M-007-012-MY3 to C. Yu). The NMR spectra were obtained at the Instrumentation Center at National Tsing Hua University (NTHU) supported by NSC of Taiwan.

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Authors and Affiliations

  1. Instrumentation Center, National Tsing Hua University, Hsinchu, Taiwan, ROC

    Kuo-Wei Hung

  2. Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan, ROC

    Chan-Chia Hsu & Chin Yu

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  1. Kuo-Wei Hung
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  2. Chan-Chia Hsu
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  3. Chin Yu
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Correspondence to Kuo-Wei Hung or Chin Yu.

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Hung, KW., Hsu, CC. & Yu, C. Solution structure of human Ca2+-bound S100A12. J Biomol NMR 57, 313–318 (2013). https://doi.org/10.1007/s10858-013-9781-3

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