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Figure 4.
Figure 4 Comparison of the KAP-1 PHD, PML RING, IEEHV RING and
RAG1 RING. Superposition of KAP-1 PHD (with blue  -strands,
aa 627 -652) and PML RING (magenta -strands,
aa 56 -81) (A) and RAG1 RING (yellow -strands,
aa 292 -317) (B) from the first metal ligand to the sixth metal
ligand. The white spheres represent zinc atoms with the upper
zinc atom being site I. The orientation of KAP-1 PHD is the same
in both panels. (C) Superposition of zinc-binding site I for
KAP-1 (627 -632, 647 -652), PML (56 -71, 76 -81), IEEHV (7 -12,
28 -33) and RAG1 (292 -297, 312 -317). The metal ligands are
colored according to protein: KAP-1 in blue, PML in magenta,
IEEHV in green and RAG1 in yellow. (D) Superposition of the
conserved hydrophobic core residues N-terminal to metal ligand 5
and C-terminal to metal ligand 6 (L76 and L81 in PML, F28 and
I33 in IEEHV, and F312, I317, F647 and H652 in PHD). The
side-chains are colored as in (C). The core residues from PHD
are noted for clarity. The conserved tryptophan within the PHD
family (W664 in KAP-1) is seen here inserting between the other
core residues, repositioning the core.
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