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Figure 2.
Fig. 2. Sequence conservation of C3d. (A) Multiple sequence
alignment of selected species of C3d and human C4d (B isotype)
(21). Residues shaded in yellow are at least 90% buried in the^
C3d structure, and those shaded in red are residues composing
the contiguous surface patch labeled in (B). Numbers correspond^
to the degree of conservation in C3d sequences only: 0 (not
conserved) to A (highly conserved), as determined by the program
AMAS (32). In human C4d, approximately 75% of the core residues,
as well as the putative domain interface residues, are highly
conserved^ [a conservation index (cons. index) of 7 or higher
when included^ in the AMAS calculation], which suggests that it
will adopt a^ similar fold and possess the analogous domain
interface. The helical segments in human C3d are indicated by
blue cylinders. [The figure^ was prepared with ALSCRIPT (35).]
(B) Mapping of residue^ conservation as determined in (A) onto
the surface of C3d; white^ (not conserved) to progressively
darker red (highly conserved). [The figure was prepared with
GRASP (36).] The conserved patch includes most of the surface
apolar residues shown in Fig. 1C.
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