Figure 2
From: Functional Diversification and Specialization of Cytosolic 70-kDa Heat Shock Proteins
HspA1A and HspA8 have highly conserved primary sequences and are structurally identical.
(a) Multiple sequence alignment of the human HspA1A and HspA8 proteins and their mice orthologs. The sequences were aligned using the MAFFT algorithm. The sequences used are: human HspA1A (HspA1A: NP_005336), mouse HspA1A (MmA1A: NP_034609), human HspA8 (HsA8: NP_006588) and mouse HspA8 (MmA8: NP_112442). The two major domains of the proteins are: the nucleotide-binding domain (NBD: amino acids 1–382) and the substrate-binding domain (amino acids 396–641). Amino acid positions 383–395 are the flexible hydrophobic linker, which connects the two domains. (b) Structural alignment between the HspA1A (grey) and HspA8 (black) NBD region showing the overall structural similarities. The structural alignment was performed using DaliLite and the figures were generated with PyMol. The PDB codes of the structures used are: 3JXU for HspA1A and 3HSC for HspA8.
