Skip to main content
. 2005 Mar;14(3):684–695. doi: 10.1110/ps.041152805

Figure 4.

Figure 4.

Superposition of the monomeric subunits of Mj sHSP16.5 (blue), wheat sHSP16.9 (green), and human αB crystallin (red). The 3D coordinates of the three structures were superimposed yielding a final RMSD of 3.25 Å. All three structures have the same basic topology. The hydrophobic N terminus is largely helical (except in Mj sHSP16.5, where the N terminus is unresolved in the X-ray structure). An immunoglobulin-like α crystallin core domain consists of β strands (11 in Mj sHSP16.5, eight in wheat sHSP16.9, and seven in αB crystallin) that form two anti-parallel β sheets connected by a flexible loop. The C-terminal extension is highly charged and unstructured. Note that the C-terminal extension is unresolved in the X-ray structure of Mj sHSP16.5.

HHS Vulnerability Disclosure