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. Author manuscript; available in PMC: 2013 Mar 1.
Published in final edited form as: Biochim Biophys Acta. 2011 Nov 3;1823(3):774–787. doi: 10.1016/j.bbamcr.2011.10.013

Figure 4. Comparisons of the linker domains of human HSP90β (hum90β) and GRP94 (hum94).

Figure 4

*, identical residues. :, similar residues. Blue, acidic residues. Red, basic residues. Purple, Asn and Gln. Green, aromatic residues. Orange, aliphatic residues. Brown, Pro. Black, small side chain residues. Strands 8 and 9, which flank much of the charged stretches and bind the domain to the N-terminal domain are indicated, and the Trp zipper domain interaction motif within strand 9 is underlined. The heavily negative sequence in the middle of the GRP94 domain is likely to contain a Ca++ binding site [92]. A human GRP94 allele has Pro300Leu substitution (yellow highlight) (http://browser.1000genomes.org/index.html, rs116891695). This sequence comparison is instructive because a 3D structure for the charged linkers has proven elusive.