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Figure 4.
Figure 4. PYRIN domain structure and distribution of
charged residues. (a) Stereo view of a superposition of the
backbone atoms in the 20 conformers representing the NMR
structure of the ASC PYRIN domain (Table 1). Numbers identify
sequence positions. (b) Stereo view of the conformer closest to
the mean structure of the 20 conformers shown in (a). The
following colors were used for the side-chains: blue, Arg, Lys,
His; red, Glu, Asp; yellow, Ala, Cys, Ile, Leu, Met, Phe, Pro,
Trp, Val; grey, Asn, Gln, Ser, Thr, Tyr. Bold lines identify
charged side-chains of Arg, Lys, Asp and Glu. The molecule is
oriented so that most of the negatively and positively charged
side chains are located, respectively, in the left and right
half of the molecule. (c) and (d) Ribbon drawing of the PYRIN
domain. Spheres identify the positions of C^a atoms, where
positively (blue) and negatively (red) charged side-chains are
located in the zebrafisch PYRIN domains of zAsc (c) and Caspy
(d). The six helices are numbered.
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