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Figure 5.
Figure 5 Binding of  2GPI
to an anionic phospholipid surface. (A) Two views, related by
180° rotation, of the electrostatic potential surface of 2GPI.
Domains are labelled I -V. The electrostatic potential is scaled
from red for negative to blue for positive. (B) Positively
charged patch on the aberrant half of domain V. The 14 residues
contributing to this patch and the position of the disordered
loop Ser311 -Lys317 are indicated. (C) Diagram of the proposed
model for binding of 2GPI
to acidic phospholipids. The positively charged patch on the
surface of domain V is indicated by '+', acidic phospholipids
are depicted by '-' and the putative membrane-insertion loop
Ser311 -Ser -Leu -Ala -Phe -Trp -Lys317 is shown to insert into
the phospholipid layer. The positions of N-glycans are indicated
by hexagons and the putative site for O-linked glycosylation is
indicated by a diamond.
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