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PDBsum entry 1kgd

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Protein binding PDB id
1kgd
Jmol
Contents
Protein chain
175 a.a. *
Ligands
FMT ×5
Waters ×218
* Residue conservation analysis
PDB id:
1kgd
Name: Protein binding
Title: Crystal structure of the guanylate kinase-like domain of human cask
Structure: Peripheral plasma membrane cask. Chain: a. Fragment: guanylate kinase like domain. Synonym: cask. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
1.31Å     R-factor:   0.188     R-free:   0.212
Authors: Y.Li,O.Spangenberg,I.Paarmann,M.Konrad,A.Lavie
Key ref:
Y.Li et al. (2002). Structural basis for nucleotide-dependent regulation of membrane-associated guanylate kinase-like domains. J Biol Chem, 277, 4159-4165. PubMed id: 11729206 DOI: 10.1074/jbc.M110792200
Date:
26-Nov-01     Release date:   19-Dec-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O14936  (CSKP_HUMAN) -  Peripheral plasma membrane protein CASK
Seq:
Struc:
 
Seq:
Struc:
926 a.a.
175 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.7.11.1  - Non-specific serine/threonine protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
ATP
+ protein
= ADP
+ phosphoprotein
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1074/jbc.M110792200 J Biol Chem 277:4159-4165 (2002)
PubMed id: 11729206  
 
 
Structural basis for nucleotide-dependent regulation of membrane-associated guanylate kinase-like domains.
Y.Li, O.Spangenberg, I.Paarmann, M.Konrad, A.Lavie.
 
  ABSTRACT  
 
CASK is a member of the membrane-associated guanylate kinases (MAGUK) homologs, a family of proteins that scaffold protein complexes at particular regions of the plasma membrane by utilizing multiple protein-binding domains. The GK domain of MAGUKs, which shares high similarity in amino acid sequence with yeast guanylate kinase (yGMPK), is the least characterized MAGUK domain both in structure and function. In addition to its scaffolding function, the GK domain of hCASK has been shown to be involved in transcription regulation. Here we report the crystal structure of the GK domain of human CASK (hCASK-GK) at 1.3-A resolution. The structure rationalizes the inability of the GK domain to catalyze phosphoryl transfer and strongly supports its new function as a protein-binding module. Comparison of the hCASK-GK structure with the available crystal structures of yGMPK provides insight into possible conformational changes that occur in hCASK upon GMP binding. These conformational changes may act to regulate hCASK-GK function in a nucleotide-dependent manner.
 
  Selected figure(s)  
 
Figure 1.
Fig. 1. Sequence alignment of the GK domain of MAGUKs and yGMPK. The alignment was done using the Multalin Interface Page and further edited manually (39). The glycine-rich ATP binding motif and residues responsible for binding of guanine ring ( ), phosphates (*) of GMP, and for binding of Mg2+(+) are boxed as well as the residues involved in catalysis (Arg-135, Arg-146, and Asn-168 in yGMPK, ) and the residue responsible for ATP binding (Arg-131).
Figure 3.
Fig. 3. Stereoviews. A, a fragment of the experimental electron density map of hCASK-GK (1.7-Å resolution) contoured at 1.5 shown superimposed with the final structure. B, overlay of the complete hCASK-GK (red), GMPK[apo] (blue), and GMPK[GMP] (cyan) structures. The superposition matrices were calculated using only the C atoms of the CORE region.
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2002, 277, 4159-4165) copyright 2002.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18809851 I.Paarmann, M.F.Lye, A.Lavie, and M.Konrad (2008).
Structural requirements for calmodulin binding to membrane-associated guanylate kinase homologs.
  Protein Sci, 17, 1946-1954.  
17220895 M.L.Reese, S.Dakoji, D.S.Bredt, and V.Dötsch (2007).
The guanylate kinase domain of the MAGUK PSD-95 binds dynamically to a conserved motif in MAP1a.
  Nat Struct Mol Biol, 14, 155-163.  
17096593 D.Korkin, F.P.Davis, F.Alber, T.Luong, M.Y.Shen, V.Lucic, M.B.Kennedy, and A.Sali (2006).
Structural modeling of protein interactions by analogy: application to PSD-95.
  PLoS Comput Biol, 2, e153.  
16879967 J.Boudeau, D.Miranda-Saavedra, G.J.Barton, and D.R.Alessi (2006).
Emerging roles of pseudokinases.
  Trends Cell Biol, 16, 443-452.  
15952887 L.Funke, S.Dakoji, and D.S.Bredt (2005).
Membrane-associated guanylate kinases regulate adhesion and plasticity at cell junctions.
  Annu Rev Biochem, 74, 219-245.  
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.