3VUT

Crystal structures of non-phosphorylated MAP2K4


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Free: 0.407 
  • R-Value Work: 0.331 
  • R-Value Observed: 0.335 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal and solution structures disclose a putative transient state of mitogen-activated protein kinase kinase 4

Matsumoto, T.Kinoshita, T.Kirii, Y.Tada, T.Yamano, A.

(2012) Biochem Biophys Res Commun 425: 195-200

  • DOI: https://doi.org/10.1016/j.bbrc.2012.07.066
  • Primary Citation of Related Structures:  
    3VUT

  • PubMed Abstract: 

    Mitogen-activated protein kinase kinase 4 (MAP2K4) plays a crucial role in the stress-activated signal cascade and is enzymatically regulated by ligand or substrate binding, and/or post-translational modification. Crystal structures combined with small-angle X-ray scattering experiments revealed that the apo form of non-phosphorylated MAP2K4 (npMAP2K4) exists in a transient state which has a longer conformation compared with the typical kinase folding. Upon ATP-binding, the transient conformation adopted the configuration of typical kinase folding. In the absence of ATP-binding, the transient state of apo npMAP2K4 may shift to a state of aggregation via non-particular hydrophobic interactions as a result of the exposed hydrophobic residues.


  • Organizational Affiliation

    Rigaku Corporation, Akishima, Tokyo 196-8666, Japan. t-matumo@rigaku.co.jp


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Dual specificity mitogen-activated protein kinase kinase 4
A, B
327Homo sapiensMutation(s): 0 
Gene Names: MAP2K4JNKK1MEK4MKK4PRKMK4SEK1SERK1SKK1
EC: 2.7.12.2
UniProt & NIH Common Fund Data Resources
Find proteins for P45985 (Homo sapiens)
Explore P45985 
Go to UniProtKB:  P45985
PHAROS:  P45985
GTEx:  ENSG00000065559 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP45985
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Free: 0.407 
  • R-Value Work: 0.331 
  • R-Value Observed: 0.335 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 67.773α = 90
b = 87.362β = 90
c = 118.373γ = 90
Software Package:
Software NamePurpose
SERGUIdata collection
MOLREPphasing
REFMACrefinement
CrystalCleardata reduction
CrystalCleardata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-09-05
    Type: Initial release
  • Version 1.1: 2017-11-22
    Changes: Refinement description
  • Version 1.2: 2024-03-20
    Changes: Data collection, Database references