 |
PDBsum entry 3a2c
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
(+ 1 more)
274 a.a.
|
|
|
|
|
|
|
|
|
|
|
287 a.a.
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Transferase
|
|
|
Title:
|
|
Crystal structure of a pyrazolopyrimidine inhibitor complex bound to mapkap kinase-2 (mk2)
|
|
Structure:
|
|
Map kinase-activated protein kinase 2. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Fragment: kinase domaine, residues 41-364. Synonym: mapk-activated protein kinase 2, mapkap kinase 2, mapkapk-2, mk2. Engineered: yes
|
|
Source:
|
|
Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
|
|
Resolution:
|
|
|
2.90Å
|
R-factor:
|
0.288
|
R-free:
|
0.335
|
|
|
Authors:
|
|
A.Fujino,M.Takimoto-Kamimura
|
|
Key ref:
|
|
A.Fujino
et al.
(2010).
Structural analysis of an MK2-inhibitor complex: insight into the regulation of the secondary structure of the Gly-rich loop by TEI-I01800.
Acta Crystallogr D Biol Crystallogr,
66,
80-87.
PubMed id:
|
|
|
Date:
|
|
|
12-May-09
|
Release date:
|
12-May-10
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
Chains A, B, C, D, E, F, G, H, I, J, K, L:
E.C.2.7.11.1
- non-specific serine/threonine protein kinase.
|
|
|
|
|
|
|
Reaction:
|
|
|
1.
|
L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
|
|
2.
|
L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
|
|
|
|
|
|
|
L-seryl-[protein]
|
+
|
ATP
|
=
|
O-phospho-L-seryl-[protein]
|
+
|
ADP
|
+
|
H(+)
|
|
|
|
|
|
|
L-threonyl-[protein]
|
+
|
ATP
|
=
|
O-phospho-L-threonyl-[protein]
|
+
|
ADP
|
+
|
H(+)
|
|
|
|
|
|
|
|
|
|
|
|
|
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
| |
|
|
Acta Crystallogr D Biol Crystallogr
66:80-87
(2010)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structural analysis of an MK2-inhibitor complex: insight into the regulation of the secondary structure of the Gly-rich loop by TEI-I01800.
|
|
A.Fujino,
K.Fukushima,
N.Namiki,
T.Kosugi,
M.Takimoto-Kamimura.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Mitogen-activated protein kinase-activated protein kinase 2 (MAPKAP-K2 or MK2)
is a Ser/Thr kinase from the p38 mitogen-activated protein kinase signalling
pathway and plays an important role in inflammatory diseases. The crystal
structure of the complex of human MK2 (residues 41-364) with the potent MK2
inhibitor TEI-I01800 (pK(i) = 6.9) was determined at 2.9 A resolution. The MK2
structure in the MK2-TEI-I01800 complex is composed of two domains, as observed
for other Ser/Thr kinases; however, the Gly-rich loop in the N-terminal domain
forms an alpha-helix structure and not a beta-sheet. TEI-I01800 binds to the
ATP-binding site as well as near the substrate-binding site of MK2. Both
TEI-I01800 molecules have a nonplanar conformation that differs from those of
other MK2 inhibitors deposited in the Protein Data Bank. The MK2-TEI-I01800
complex structure is the first active MK2 with an alpha-helical Gly-rich loop
and TEI-I01800 regulates the secondary structure of the Gly-rich loop.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
|
Links
