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Calendar Name: seminars
Scheduled for: Monday, November 7 2011, 11:00 - 12:30
Event text:    Prof Peter Tompa
	       
	       VIB Department of Structural Biology
	       Vrije Universiteit Brussel
	       
	       Brussel
	       BELGIUM
Details:       “Intrinsically disordered proteins in cellular function
	       and disease”
	       
	       ABSTRACT
	       Peter Tompa1,2
	       1VIB Department of Structural Biology, Brussels and
	       2Institute of Enzymology, Budapest
	       Our traditional view of proteins is rooted in the notion
	       that a well-defined three-dimensional structure is the
	       prerequisite of their function. The evidence is steadily
	       growing, however, that for a significant fraction of the
	       proteome the functionally relevant state is not
	       structured [1,2]. This recognition has called for the
	       extension of the protein structure-function paradigm to
	       encompass such proteins and protein domains, now termed
	       intrinsically unstructured, intrinsically disordered
	       (IDPs) or natively unfolded. Here the current state of
	       this rapidly advancing field is surveyed [3]. It is
	       shown that such proteins are common in living organisms
	       and play important roles in the regulation of key
	       cellular processes of signaling and transcription. It
	       will be shown that we have multiple experimental
	       techniques at our disposal for the characterization of
	       the structural ensemble of IDPs, and also that
	       structural disorder provides advantages so that IDPs
	       often surpass globular proteins in terms of functional
	       specificity, versatility, speed and control [4]. Because
	       of their important functions, however, IDPs are also
	       often involved in disease, such as cancer and
	       neurodegeneration. Thus, it is argued that understanding
	       this structural phenomenon at atomic resolution not only
	       represents a novel challenge for extending the
	       structure-function paradigm, but also presents novel
	       targets and raises new hope for drug discovery [5].
	       
	       [1]     Tompa, P. (2002) Intrinsically unstructured
	       proteins. Trends Biochem. Sci. 27, 527-533.
	       [2]     Tompa, P. (2009) Structure and function of
	       intrinsically disordered proteins, CRC Press (Taylor and
	       Francis Group), Boca Raton, Fl.
	       [3]     Tompa, P. (2011) Unstructural biology coming of
	       age. Curr. Opin. Struct. Biol. 21, 419-25.
	       [4]     Kovacs, D., Kalmar, E., Torok, Z. and Tompa, P.
	       (2008) Chaperone activity of ERD10 and ERD14, two
	       disordered stress-related plant proteins. Plant Physiol.
	       147, 381-90.
	       [5]     Metallo, S.J. (2010) Intrinsically disordered
	       proteins are potential drug targets. Curr. Opin. Chem.
	       Biol. 14, 481-8.

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