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. Author manuscript; available in PMC: 2009 Feb 1.
Published in final edited form as: J Mol Biol. 2007 Nov 22;375(5):1197–1205. doi: 10.1016/j.jmb.2007.11.036

Figure 4.

Figure 4

Hydrophobic core of the opened region of assembled HIP1 is disrupted by hydrophilic amino acids in a- and d-positions of the heptad repeat. The domain map of the assembled HIP1 model (371-587) is divided into coiled-coil regions A (red) and B (yellow) and an opened segment, designated region C (pink). N and C-term are the N- and C-terminal ends. Amino acids that occupy a- and d-positions (predicted by COILS 35) in regions A, B, and C are in bold capital letters and the a-position residue numbers are indicated above the a labels. Asterisks indicate skips in the heptad repeat flagged by COILS. Boxed amino acids in A, B, and C are disruptive to the hydrophobic core (see text). Region A: there are two coiled-coil stabilizing clusters (underlined, see text) separated by S398. Region B: the underlined LLI sequence may represent an altered coiled-coil cluster with glycine at position 524 instead of leucine. Changing G524 to L (indicated by the arrow) would create a stabilizing coiled-coil cluster (LLIL) seen in myosin 29.