structural biology      

 

Juha Rouvinen


Born 1960, M.Sc. 1986 (University of Joensuu), Ph.Lic. 1987, Graduate student (University of Uppsala) 1987-1990, PhD 1991 (University of Joensuu), Docent 1993 (University of Kuopio), Senior Assistant (University of Joensuu) 1993-1996, Senior Researcher (Academy of Finland) 1996-2001, Professor (University of Joensuu/Eastern Finland) 2001-. Dean of the Faculty 2007-2009.

Research interests

Three-dimensional structures and functional mechanisms of proteins.

Research highligts

Rouvinen J, Bergfors T, Teeri T, Knowles J & Jones TA: Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. Science 249 (1990) 380-386. Describes the first three-dimensional structure of cellulose digesting enzyme and suggests how enzyme works.

Oinonen C, Tikkanen R, Rouvinen J & Peltonen L: Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nature Struct. Biol. 2 (1995) 1102-1108. Describes the first three-dimensional structure of aspartylglucosaminidase and analyses possible structural consequences of mutations leading to the human genetic disease aspartylglucosaminuria.

Hakulinen N, Kiiskinen L-L, Kruus K, Saloheimo M, Koivula A & Rouvinen J: Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site. Nature Struct. Biol. 9 (2002) 601-605. Describes the first fully active three-dimensional structure of laccase which participates in lignin degradation. The structure revealed a novel binding mode of dioxygen in the trinuclear copper site in which dioxygen is reduced to water.

Hakanpää J, Linder M, Askolin S, Nakari-Setälä T, Parkkinen T, Penttilä M & Rouvinen J: Atomic resolution structure of the HFBII hydrophobin: a self-assembling amphiphile. J. Biol. Chem. 279 (2004) 527-533. Describes the first three-dimensional structure of hydrophobin which has a novel fold and amphiphilic surface which affects hydrophobin's function to form assemblies, monolayers and reduce surface tension.

Rouvinen J, Jänis J, Laukkanen M-L, Jylhä, S, Niemi, M, Päivinen T, Mäkinen-Kiljunen S, Haahtela T, Söderlund H & Takkinen K: Transient dimers of allergens. PLoS ONE 5 (2010) e9037. By using crystal structure analysis and native mass spectrometry it was found that number of allergens are able to form dimers which increase the presentation of identical IgE-epitopes and consequently allergens capacity to trigger degranulation in immediate allergic reaction. The work has led to the foundation of Desentum company which develops new hypoallergens for allergen-specific immunotherapy.