Figure 1.
Figure 1: Overall structure of the ZP-N domain of ZP3. a,
Cartoon representation rainbow-coloured from blue (N terminus)
to red (C terminus), with conserved disulphides shown as grey
sticks. b, Topology, with strands as triangles, and helices as
circles. Connections between secondary structure elements at the
top, middle or bottom of the structure are represented by
straight continuous, rounded dashed and straight dashed lines,
respectively. c, Structure-based alignment of ZP-N sequences of
mouse (m) and human (h) zona pellucida proteins, as well as
non-egg coat ZP domain proteins -tectorin
(TECTA), endoglin (ENG) and uromodulin (UMOD). Consensus
sequences (cons.) for ZP3 homologues and Pfam ZP domain family
seed sequences are also shown (for colour-coding and consensus
keys, see Methods). Brown circles mark residues in which the
side chains lie on the inner side of -sheets;
open and closed black boxes indicate conserved hydrophobic core
and Cys residues, respectively.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2008,
456,
653-657)
copyright 2008.
-tectorin
(TECTA), endoglin (ENG) and uromodulin (UMOD). Consensus
sequences (cons.) for ZP3 homologues and Pfam ZP domain family
seed sequences are also shown (for colour-coding and consensus
keys, see Methods). Brown circles mark residues in which the
side chains lie on the inner side of 
-sheets;
open and closed black boxes indicate conserved hydrophobic core
and Cys residues, respectively.