 |
PDBsum entry 1bdy
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Calcium-binding
|
PDB id
|
|
|
|
1bdy
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of the c2 domain from protein kinase c-Delta.
|
|
|
Authors
|
|
H.Pappa,
J.Murray-Rust,
L.V.Dekker,
P.J.Parker,
N.Q.Mcdonald.
|
|
|
Ref.
|
|
Structure, 1998,
6,
885-894.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
BACKGROUND: The protein kinase C (PKC) family of lipid-dependent serine/theonine
kinases plays a central role in many intracellular eukaryotic signalling events.
Members of the novel (delta, epsilon, eta, theta) subclass of PKC isotypes lack
the Ca2+ dependence of the conventional PKC isotypes and have an N-terminal C2
domain, originally defined as V0 (variable domain zero). Biochemical data
suggest that this domain serves to translocate novel PKC family members to the
plasma membrane and may influence binding of PKC activators. RESULTS: The
crystal structure of PKC-delta C2 domain indicates an unusual variant of the C2
fold. Structural elements unique to this C2 domain include a helix and a
protruding beta hairpin which may contribute basic sequences to a
membrane-interaction site. The invariant C2 motif, Pro-X-Trp, where X is any
amino acid, forms a short crossover loop, departing radically from its
conformation in other C2 structures, and contains a tyrosine phosphorylation
site unique to PKC-delta. This loop and two others adopt quite different
conformations from the equivalent Ca(2+)-binding loops of phospholipase C-delta
and synaptotagmin I, and lack sequences necessary for Ca2+ coordination.
CONCLUSIONS: The N-terminal sequence of Ca(2+)-independent novel PKCs defines a
divergent example of a C2 structure similar to that of phospholipase C-delta.
The Ca(2+)-independent regulation of novel PKCs is explained by major structural
and sequence differences resulting in three non-functional Ca(2+)-binding loops.
The observed structural variation and position of a tyrosine-phosphorylation
site suggest the existence of distinct subclasses of C2-like domains which may
have evolved distinct functional roles and mechanisms to interact with lipid
membranes.
|
|
|
|
|
|
Figure 2.
Figure 2. Isomorphous and anomalous difference Fourier maps
using selenomethionine data, superimposed on a backbone
representation of the two molecules within the asymmetric unit.
Experimental phases from the two mercury derivatives were used
in map calculation; both maps are contoured at 5s. The ten
selenium sites in the asymmetric unit are labelled according to
the methionine residue number. (The figure was produced using
the program SETOR [40].)
|
|
|
|
|
|
The above figure is
reprinted
by permission from Cell Press:
Structure
(1998,
6,
885-894)
copyright 1998.
|
|
|
|
|
|
|
