Figure 2.
Fig. 2. The interaction between NGF and p75. (A) Close-up of
the site I interface (NGF monomer A is green; monomer B, blue;
and p75, purple). The backbone is depicted as tubes, and side
chains are depicted as sticks. The buried salt bridge between
NGF Lys88A and p75 Asp41 in site I is highlighted by thickened
side chains. (B) Close-up of the site II interface. (C) Charge
complementarity between the acidic p75 and the basic NGF dimer
is shown as their respective GRASP surfaces. Acidic is red and
basic is blue. (D) A representative electron density map ( A
2F[obs] - F[calc]) around the patch 1 of site I, showing the
knob-in-hole surface complementarity. (E) NT sequence alignment
showing that the p75 contact residues are conserved across all
NTs. Monomer A residues are shaded in green and monomer B
residues shaded in blue. Site I residues are labeled "1," and
site II residues are labeled "2".
The above figure is reprinted
by permission from the AAAs:
Science
(2004,
304,
870-875)
copyright 2004.
A
2F[obs] - F[calc]) around the patch 1 of site I, showing the
knob-in-hole surface complementarity. (E) NT sequence alignment
showing that the p75 contact residues are conserved across all
NTs. Monomer A residues are shaded in green and monomer B
residues shaded in blue. Site I residues are labeled "1," and
site II residues are labeled "2".