Figure 4
From: Domain swapping and SMYD1 interactions with the PWWP domain of human hepatoma-derived growth factor
Comparisons of B-factors at regions with large structural differences between the complex and the apo forms. (A) The overall B-factor of the PWWP-SMYD1 complex is less than that of the apo PWWP domain. (B) The B-factors of the residues on the hinge loop in the apo form (right panel) are much greater than that of the newly formed αC in the complex (left). (C) The B-factors of the region with the deformed αA (Pro60 – Asp62) and newly formed β5 (Leu63 – Pro65) in the PWWP-SMYD1 complex (left) are less than that in the apo form (right). (D) The flexibility of DNA-binding loops in the complex (left) is less than that in the apo form (right). (E) The B-factors of the residues involved in hydrogen bonding in the swapped C/N terminus of the complex (left) are less than those in the apo PWWP domain (right). The residues involved in each compared region are presented as sticks.
