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. Author manuscript; available in PMC: 2011 Jul 23.
Published in final edited form as: J Mol Biol. 2010 May 19;400(4):702–714. doi: 10.1016/j.jmb.2010.05.022

Figure 1. CaM-binding sites on the MA structure.

Figure 1

(Top) Amino acid sequence for the MA construct used in this experiment, depicting the proposed CaM-binding sites (underlined) and the tryptophan residues located within (bold). a) Surface depiction of the MA NMR structure (PDB: 2HMX) showing the tryptophan residues (black) located within the N-terminal lobe of MA, with W16 completely buried within the hydrophobic core while W36 is partially exposed to solvent. b) Closeup view of the N-terminal globular domain of MA and the CaM-binding site (blue) in cartoon form. The site is composed of two short α-helices connected by a basic loop region.