The interplay between structure and function in intrinsically unstructured proteins |
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Authors: | Tompa Peter |
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Affiliation: | Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P.O. Box 7, H-1518 Budapest, Hungary. tompa@enzim.hu |
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Abstract: | Intrinsically unstructured proteins (IUPs) are common in various proteomes and occupy a unique structural and functional niche in which function is directly linked to structural disorder. The evidence that these proteins exist without a well-defined folded structure in vitro is compelling, and justifies considering them a separate class within the protein world. In this paper, novel advances in the rapidly advancing field of IUPs are reviewed, with the major attention directed to the evidence of their unfolded character in vivo, the interplay of their residual structure and their various functional modes and the functional benefits their malleable structural state provides. Via all these details, it is demonstrated that in only a couple of years after its conception, the idea of protein disorder has already come of age and transformed our basic concepts of protein structure and function. |
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Keywords: | CBP, CREB-binding protein CD, circular dichroism CREB, cAMP response element binding protein Cdk, cyclin-dependent kinase CST, calpastatin DHPR, dihydropyridine receptor FTIR, Fourier-transformed infrared spectroscopy IUP, intrinsically unstructured protein KID, kinase-inducible domain MAP2, microtubule-associated protein 2 MoRE, molecular recognition element NACP, non-A beta component of Alzheimer’s disease amyloid plaque (also termed α-synuclein) NMR, nuclear magnetic resonance PCS, primary contact site PEVK, region rich in Pro, Glu, Val and Lys PP II, polyproline II helix RNAP II, DNA-dependent RNA polymerase II ROA, Raman optical activity SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis |
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