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Proteopedia entry: Coiled‐coil structure of keratins
Author(s) -
Hanukoglu Israel,
Ezra Liora
Publication year - 2013
Publication title -
biochemistry and molecular biology education
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.34
H-Index - 39
eISSN - 1539-3429
pISSN - 1470-8175
DOI - 10.1002/bmb.20746
Subject(s) - keratin , intermediate filament , cytoskeleton , coiled coil , protein secondary structure , helix (gastropod) , biology , alpha helix , protein structure , keratin 6a , protein filament , sequence (biology) , biochemistry , crystallography , chemistry , biophysics , genetics , ecology , snail , cell
Type I and type II keratins represent a large family of proteins that are encoded by 54 genes in the human genome. Matched pairs of these keratins form heterodimers that constitute the basic building blocks of cytoskeletal intermediate filaments and epidermal derivatives of hair, nail and horn. Keratins have an important place in the history of the elucidation of protein structure as in 1951, Pauling et al. suggested the first model for a-helix structure for wool a-keratins, in the absence of knowledge of the sequence of keratins [1]. The first sequence of a cytoskeletal keratin was determined in 1982 [2]. By analyzing the sequences of type I and type II keratins using secondary structure prediction methods Hanukoglu and Fuchs suggested a model for the structure of keratins and other intermediate filaments proteins [3]. This model depicted a conserved central 310 residue long rod with four helical domains and highly variable N and C terminal domains that were suggested to participate in linking of subunits and interaction with other proteins. Keratins are very difficult to solubilize as they readily form clusters even in denaturing urea solutions. To partially overcome this problem in 2012, Lee et al. coexpressed the longest helical segment 2B from a pair of keratins (K14 and K5) and determined the first crystal structure of a keratin helical segment [4]. The coiled-coil helical structure of this 2B segment is shown in Fig. 1. This structure confirms the four helix model suggested by secondary structure predictions [3]. The Proteopedia entry presents interactive views of the keratin helical structure and the roles of hydrophobic residues as opposed to charged residues in the formation of coiled-coil structure of filaments. Incorporation of keratins in biochemistry and molecular biology courses could contribute to the understanding of the principles of protein structure, families of homologous proteins and the evolution of the genes that encode for them, and formation of the cytoskeletal scaffold in cell biology. Coiled-coil structures are widespread in the biological world [5], and keratins represent simple examples to illustrate the forces that bind these structures. Sequence based prediction of keratin structural domains can be taught as an illustrative example of the usefulness of protein structure prediction methods.