Figure 1.
Figure 1: Ribbon diagrams of HFE, TfR and HFE-TfR structures.
a, HFE^5 (PDB code 1A6Z). Residues substituted in HH mutations
(Cys 260 and His 41)3 and a cluster of histidines (residues 87,
89, 94 and 123) are highlighted. An arrow indicates the inward
displacement of 1
domain helix as compared with the analogous class I MHC helix.
b, TfR monomer from homodimer structure^15 (made using
coordinates provided by C. M. Lawrence and S. C. Harrison). A,
apical loop (residues 312-328); PL, protease-like loop (residues
469-476); C tail, C-terminal tail (residues 750-760). c, Two
views of the HFE-TfR structure related by a 90° rotation about
the vertical axis. Chain termini nearest the predicted
transmembrane region (C terminus for HFE heavy chain; N terminus
for TfR) are labelled (left). The membrane bilayer is
represented by a grey box (right).
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2000,
403,
46-53)
copyright 2000.
1
domain helix as compared with the analogous class I MHC helix.
b, TfR monomer from homodimer structure^15 (made using
coordinates provided by C. M. Lawrence and S. C. Harrison). A,
apical loop (residues 312-328); PL, protease-like loop (residues
469-476); C tail, C-terminal tail (residues 750-760). c, Two
views of the HFE-TfR structure related by a 90° rotation about
the vertical axis. Chain termini nearest the predicted
transmembrane region (C terminus for HFE heavy chain; N terminus
for TfR) are labelled (left). The membrane bilayer is
represented by a grey box (right).