HSP27: Figures

Figure 1. Structures of α-Crystallins cABC and cHspB1 and their conserved domains.

A) Two Ig-like cABC monomers assemble into a dimer through pairwise and antiparallel interactions between extended β6+7 strands.(Inset) The palindromic C-terminal peptide binds to a hydrophobic groove between the β4 and β8 strands, in an antiparallel direction to the β8 strand. The N-to-C direction is illustrated by the yellow arrow. B) The crystal structure of cHspB1 reveals a dimer similar to cABC, rich in β-sheet structure and with C-terminal peptides bound. (Inset). C) Linear representation of HSPB1. α-Crystallin domain is represented by the yellow cylinder and arrows indicate the phosphorylation sites by Portein Kinases A, G and C (PKA, PKG and PKC) and Mitogen- Activated Protein Kinases (MK2/3/5). (Adapted from Mymrikov et. al, 2010 and Hochberg et.al, 2014 ).^38,24 D) Three dimentional structure of HspB1, Default element colours are as defined by PyMOL e.g.carbon, nitrogen, oxygen, sulphur, phosphorus, selenium. Positively and negatively-charged atoms of standard residues in proteins and polynucleotides are blue and red respectively. Similarly, electro-positive and electro-negative polar atoms are skyblue and salmon respectively.