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Figure 1.
Figure 1 Crystal structure of the erythropoietin-(EPObp)[2]
complex.  -Helices
are shown as red cylinders and  -sheets
as green ribbons. Erythropoietin: A(8-26)
up, B'(47-52),
B(55-83)
up, C(90-112)
down, C'(114-121),
D(138-161)
down, 1(39-41),
2(133-135).
Disulphide bridges: Cys 7-Cys 161, Cys 29-Cys 33. D1 domain of
EPObp: 1(9-22),
A(26-30),
B(36-42),
C(52-59),
C'(65-68),
D(69-74),
E(78-85),
F(95-103),
G(106-113).
Disulphide bridges: Cys 28-Cys 38, Cys 67-Cys 83. D2 domains of
EPObp: A(119-132),
B(137-143),
C(154-162),
C'(170-174),
E(179-183),
F(190-201),
G(216-220).
EPObp loops that interact with erythropoietin are labelled
L1(31-35), L2(60-64), L3(86-94), L4(114-118), L5(144-153) and
L6(202-205). The locations of residues in the WSXWS box,
dimerizing mutation site^23 R130C, two Asn  arrow
Gln mutation sites (52, 164) on EPObp, and three Asn arrow
Lys mutations (24, 38, 83) on erythropoietin are depicted as
white spheres. EPO, erythropoietin.
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