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Figure 6.
FIGURE 6. Showcase of mutations. A, studies failed to
detect any effect of the V458M polymorphism, although the
conserved hydrophobic core (around strands s2B, s3B, and s4B) is
involved (53). The reason is that the side chain of Met^458
(space-filled) sits in the biggest cavity of rC1-inh (orange
cloud); hence, spatial differences are tolerated. B, the A436T
mutation affects a residue whose side chain becomes buried upon
RCL incorporation. Similar mutants of other serpins usually
result in cleavable noninhibitory serpins, because loop
insertion is hindered. Unexpectedly, the A436T mutant C1-inh is
found predominantly in noncleavable loop-inserted forms (51). In
the modeled mutant structure, the side chain of Thr^436 forms a
novel hydrogen bond network with the side chain of His^421 and
the backbone of Gln^422. This makes the RCL-inserted protein
more stable.
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