 |
PDBsum entry 3t6g
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Signaling protein, cell adhesion
|
PDB id
|
|
|
|
3t6g
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
299 a.a.
|
|
|
|
|
|
|
|
|
|
|
134 a.a.
|
|
|
|
|
|
|
|
|
|
|
273 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Nsp-Cas protein structures reveal a promiscuous interaction module in cell signaling.
|
|
|
Authors
|
|
P.D.Mace,
Y.Wallez,
M.K.Dobaczewska,
J.J.Lee,
H.Robinson,
E.B.Pasquale,
S.J.Riedl.
|
|
|
Ref.
|
|
Nat Struct Biol, 2011,
18,
1381-1387.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Members of the novel SH2-containing protein (NSP) and Crk-associated substrate
(Cas) protein families form multidomain signaling platforms that mediate cell
migration and invasion through a collection of distinct signaling motifs.
Members of each family interact via their respective C-terminal domains, but the
mechanism of this association has remained enigmatic. Here we present the
crystal structures of the C-terminal domain from the NSP protein BCAR3 and the
complex of NSP3 with p130Cas. BCAR3 adopts the Cdc25-homology fold of Ras GTPase
exchange factors, but it has a 'closed' conformation incapable of enzymatic
activity. The structure of the NSP3-p130Cas complex reveals that this closed
conformation is instrumental for interaction of NSP proteins with a focal
adhesion-targeting domain present in Cas proteins. This enzyme-to-adaptor
conversion enables high-affinity, yet promiscuous, interactions between NSP and
Cas proteins and represents an unprecedented mechanistic paradigm linking
cellular signaling networks.
|
|
|
|
|
|
|
