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Figure 1.
Figure 1. Structures of EH[2] in complex with NPF[Hrb] and with
NPF[Hrb(L  arrow
R)]. a, Stereo view showing C  traces
of 20 superimposed NMR structures of the EH[2] -NPF[Hrb(L arrow
R)] complex. The backbone C', N, and C atoms
of residues 145 -175 of EH[2], which include helices B
and C,
were used for superposition. The TNPFR sequence of NPF[Hrb(L
arrow
R)] is indicated in black. The backbone of EH[2] is color coded
as follows: helix A
consists of residues 126 -136 and is depicted in dark blue; B,
148 -156, in orange; C,
162 -172, in red; and D,
182 -197, in light blue. Loops connecting the helices are
indicated in different shades of green. The calcium ion in the
second EF-hand is represented as an orange sphere. N and C
indicate the N- and C-termini of EH[2], respectively. b, Stereo
view showing C traces
of 20 superimposed NMR structures of the EH[2] -NPF[Hrb] complex
using the same color scheme as in (a). The slightly different
orientation of the Phe side chain in the structures can be
attributed to a few NOEs that could not be assigned in spectra
of EH[2] -NPF[Hrb] due to spectral overlap. c, Ribbon and
surface representation of EH[2] -NPF[ Hrb(L arrow
R)]. The TNPFR part of the peptide is shown with C, N and O
atoms colored yellow, blue and red, respectively. The Phe and +3
residue HN protons that interact with the Asn side chain oxygen
atoms are shown in white. Val 151, Leu 155, Leu 165 and Trp 169
at the base of the NPF binding site of EH[2] are displayed as
stick models in green. The helices are color coded as in (a). d,
Ribbon and surface diagram of EH[2] -NPF[Hrb] using the same
color scheme as in ( c).
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