Biology Reference
In-Depth Information
Fig. 4.
Structure of the asymmetric dimer composed of P3A and P3B, as
shown by a surface representation of the P3A molecule (right, gray) and the
C
-trace of the P3B molecule (left, green), as viewed from the inside of the
virus particle. Regions involved in hydrogen bonding or in a salt bridge
between the P3 monomers are colored orange (P3A) and red (P3B). The
extent of each of three deletions (to residues 10, 29, and 52) is indicated.
The representation was produced with the DINO visualization program
(http://www.dino3d.org) and rendered with the Povray graphics program
(http://www.povray.org) (reproduced with permission).
9
α
the overall conformation of P3 and/or for the specific interactions
between P3A and P3B that are essential for the self-assembly of CLPs.
In the presence of MgCl
2
the stability of CLPs generated from
full-length P3 and that of intact RDV particles were the same, and par-
ticles of both types were completely dissociated by 2.6 M MgCl
2
. By
contrast, CLPs prepared from N10del-P3 were dissociated by 2.4 M
MgCl
2
and CLPs prepared from N29del-P3 were even more sensitive
to MgCl
2
. Most of the CLPs prepared from N29del-P3 were dissociated
by 2.0 M MgCl
2
and all were completely destroyed by treatment with
2.2 M MgCl
2
. These results indicated that the amino-terminal 29 amino
