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Figure 2.
Figure 2. Location of M84, M102 and M118 at the NTF2
dimerization interface. An illustration of the side-chains
protruding into the interaction interface between NTF2 chains in
the dimer. Methionine residues 84, 102 and 118 are all important
components of the hydrophobic centre of the interaction
interface. Hydrophobic residues are in grey, acidic residues in
red, basic residues in blue and amphipolar residues in white.
Also shown are the corresponding side-chains in the putative
structures (see Suyama et al.[24]) of TAP1 and NXT1. Note that
neither TAP1 nor NXT1 contains the equivalent of His100 in NTF2.
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