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Figure 2.
Fig. 2. Structure of the cpSRP43/L18p complex. (A) LHCP
topology with three transmembrane helices (TM1 to 3). The
sequence of the L18 region is given for the major LHCP, Lhcb1
from Pisum sativum, which was used in this study (red, the DPLG
motif is underlined). TM3 starts immediately after the L18
region. (B) Typical isothermal titration calorimetry (ITC)
experiment of the cpSRP43 interaction with L18p. (C) Ribbon
representation of cpSRP43 (blue) with bound L18p (as a
ball-and-stick model, gray). The N- and C-termini are indicated.
(D) Surface representation of the cpSRP43/L18p complex. The
peptide (labeled by residue numbers) binds in the hydrophobic
groove 1. Four residues at the N terminus and two residues at
the C terminus are not resolved.
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