PDBsum entry 1lez

Transferase

PDB id: 1lez

Contents

Protein chain

343 a.a. *

Ligands

LYS-LYS-ASP-LEU-ARG-ILE-SER-CYS

Waters ×110

* Residue conservation analysis

PDB id:

1lez

Name:

Transferase

Title:

Crystal structure of map kinase p38 complexed to the docking site on its activator mkk3b

Structure:

Mitogen-activated protein kinase 14. Chain: a. Synonym: map kinase p38, mitogen-activated protein kinase p38, crk1. Engineered: yes. Mutation: yes. Map kinase kinase 3b. Chain: b. Synonym: mkk3b. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Gene: p38. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes

Biol. unit:

Dimer (from PQS)

Resolution:

2.30Å R-factor: 0.216 R-free: 0.249

Authors:

C.-I.Chang,B.-E.Xu,R.Akella,M.H.Cobb,E.J.Goldsmith

Key ref:

C.I.Chang et al. (2002). Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b. Mol Cell, 9, 1241-1249. PubMed id: 12086621 DOI: 10.1016/S1097-2765(02)00525-7

Date:

10-Apr-02 Release date: 10-Jul-02

Protein chain

P47811  (MK14_MOUSE) -  Mitogen-activated protein kinase 14 from Mus musculus

Seq: 360 a.a.

Struc: 343 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.11.24 - mitogen-activated 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⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/S1097-2765(02)00525-7

Mol Cell 9:1241-1249 (2002)

PubMed id: 12086621

Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b.

C.I.Chang, B.E.Xu, R.Akella, M.H.Cobb, E.J.Goldsmith.

ABSTRACT

The structures of the MAP kinase p38 in complex with docking site peptides containing a phi(A)-X-phi(B) motif, derived from substrate MEF2A and activating enzyme MKK3b, have been solved. The peptides bind to the same site in the C-terminal domain of the kinase, which is both outside the active site and distinct from the "CD" domain previously implicated in docking site interactions. Mutational analysis on the interaction of p38 with the docking sites supports the crystallographic models and has uncovered two novel residues on the docking groove that are critical for binding. The two peptides induce similar large conformational changes local to the peptide binding groove. The peptides also induce unexpected and different conformational changes in the active site, as well as structural disorder in the phosphorylation lip.

Selected figure(s)

Figure 3.
Figure 3. Structural Details of the Docking Site RecognitionStereo diagram of the docking groove showing p38 residues (yellow) involved in interaction with (A) pepMEF2A (green) and (B) pepMKK3b (pink). Hydrogen bonds are indicated by dotted lines.

Figure 5.
Figure 5. Structure-Based Sequence Alignments of the φ[A]-X-φ[B] Docking Sites and the Docking Grooves of MAP KinasesIn (A), the basic residues and φ residues are shown in blue and orange letters, respectively. In (B), residues in p38α and equivalent residues in ERK2 and JNK2 that may participate in hydrophobic contacts with the MAP kinase docking sites are shown in orange letters.

The above figures are reprinted by permission from Cell Press: Mol Cell (2002, 9, 1241-1249) copyright 2002.

Figures were selected by an automated process.