|
Figure 3.
Fig. 3. (a) The Tyr corner, which is an important feature in
other domains, is replaced to Leu63 in AIM1g1. There are no
major effects on the fold of the molecule in spite of this
mutation. (b) The Trp corner, one of the features conserved
among AIM1g1 and lens crystallins, and its interactions in
the hydrophobic core. It acts as a bridge between A and B
motifs. (c) Surface representation of AIM1g1 showing strong
electronegative charge distribution in the loop region of the
domain. Surface representation was done using GRASP.^24 (d)
Extensive water networking is observed in the loop region. Water
molecules involved in formation of hydrogen-bond connectivities
are w118, w121, w126, w128 w147, w151, w157, w161, w171, w190,
w212 and w216 along with a glycerol molecule found in the
vicinity of the loop. These water molecules bridge the side
chains, main-chain atoms and help in stabilization. These
interactions are in addition to the electrostatic interactions
that hold crystal lattice intact.
|
