PDBsum entry 1urf

Go to PDB code: 
protein links
Transferase PDB id
Protein chain
81 a.a. *
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Hr1b domain from prk1
Structure: Protein kinasE C-like 1. Chain: a. Fragment: hr1b, residues 122-199. Synonym: plk1_human, protein-kinasE C-related kinase 1, protein kinasE C-like pkn, serine-threonine protein kinase n. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
NMR struc: 24 models
Authors: D.Owen,P.N.Lowe,D.Nietlispach,C.E.Brosnan,D.Y.Chirgadze, P.J.Parker,T.L.Blundell,H.R.Mott
Key ref:
D.Owen et al. (2003). Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1). J Biol Chem, 278, 50578-50587. PubMed id: 14514689 DOI: 10.1074/jbc.M304313200
29-Oct-03     Release date:   06-Nov-03    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q16512  (PKN1_HUMAN) -  Serine/threonine-protein kinase N1
942 a.a.
81 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Protein kinase C.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
+ protein
+ phosphoprotein
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     signal transduction   1 term 


DOI no: 10.1074/jbc.M304313200 J Biol Chem 278:50578-50587 (2003)
PubMed id: 14514689  
Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1).
D.Owen, P.N.Lowe, D.Nietlispach, C.E.Brosnan, D.Y.Chirgadze, P.J.Parker, T.L.Blundell, H.R.Mott.
PRK1 is a serine/threonine kinase that belongs to the protein kinase C superfamily. It can be activated either by members of the Rho family of small G proteins, by proteolysis, or by interaction with lipids. Here we investigate the binding of PRK1 to RhoA and Rac1, two members of the Rho family. We demonstrate that PRK1 binds with a similar affinity to RhoA and Rac1. We present the solution structure of the second HR1 domain from the regulatory N-terminal region of PRK1, and we show that it forms an anti-parallel coiled-coil. In addition, we have used NMR to map the binding contacts of the HR1b domain with Rac1. These are compared with the contacts known to form between HR1a and RhoA. We have used mutagenesis to define the residues in Rac that are important for binding to HR1b. Surprisingly, as well as residues adjacent to Switch I, in Switch II, and in helix alpha5, it appears that the C-terminal stretch of basic amino acids in Rac is required for a high affinity interaction with HR1b.
  Selected figure(s)  
Figure 1.
FIG. 1. Schematic of PRK1 showing the amino acid coordinates of the basic region (BR), HR1 repeats (HR1a, -b, and -c), pseudo-substrate site, arachidonic acid (AA) binding region, and the kinase catalytic domain. Domain limits are taken from the Pfam data base.
Figure 6.
FIG. 6. a, model of the HR1b/Rac structure generated using the HADDOCK protocols (53). The HR1b binds at a site that corresponds to Contact I in the RhoA/HR1a crystal structure. b, the crystal structure of HR1a with RhoA showed that HR1a can potentially bind to two sites on the G protein, which are designated Contact I and Contact II.
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 50578-50587) copyright 2003.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21264269 R.J.Perrin, R.Craig-Schapiro, J.P.Malone, A.R.Shah, P.Gilmore, A.E.Davis, C.M.Roe, E.R.Peskind, G.Li, D.R.Galasko, C.M.Clark, J.F.Quinn, J.A.Kaye, J.C.Morris, D.M.Holtzman, R.R.Townsend, and A.M.Fagan (2011).
Identification and validation of novel cerebrospinal fluid biomarkers for staging early Alzheimer's disease.
  PLoS One, 6, e16032.  
16611232 A.Haraga, and S.I.Miller (2006).
A Salmonella type III secretion effector interacts with the mammalian serine/threonine protein kinase PKN1.
  Cell Microbiol, 8, 837-846.  
17059209 E.Casal, L.Federici, W.Zhang, J.Fernandez-Recio, E.M.Priego, R.N.Miguel, J.B.DuHadaway, G.C.Prendergast, B.F.Luisi, and E.D.Laue (2006).
The crystal structure of the BAR domain from human Bin1/amphiphysin II and its implications for molecular recognition.
  Biochemistry, 45, 12917-12928.
PDB code: 2fic
15654870 A.D.van Dijk, R.Boelens, and A.M.Bonvin (2005).
Data-driven docking for the study of biomolecular complexes.
  FEBS J, 272, 293-312.  
16307476 A.Eberth, R.Dvorsky, C.F.Becker, A.Beste, R.S.Goody, and M.R.Ahmadian (2005).
Monitoring the real-time kinetics of the hydrolysis reaction of guanine nucleotide-binding proteins.
  Biol Chem, 386, 1105-1114.  
15260990 H.Y.Ho, R.Rohatgi, A.M.Lebensohn, Le Ma, J.Li, S.P.Gygi, and M.W.Kirschner (2004).
Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex.
  Cell, 118, 203-216.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.