PDBsum entry 3kld

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protein ligands Protein-protein interface(s) links
Cell adhesion PDB id
Protein chains
376 a.a. *
262 a.a. *
NAG ×4
Waters ×415
* Residue conservation analysis
PDB id:
Name: Cell adhesion
Title: Ptprg cntn4 complex
Structure: Contactin 4. Chain: a. Fragment: ig domains 1-4 (unp residues 25-404). Synonym: axcam, big-2. Engineered: yes. Receptor-type tyrosine-protein phosphatase gamma. Chain: b. Fragment: carbonic anhydrase-like domain (unp residues 55-3 synonym: protein-tyrosine phosphatase gamma, r-ptp-gamma.
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: cntn4. Expressed in: homo sapiens. Expression_system_taxid: 9606. Gene: ptprg. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.00Å     R-factor:   0.182     R-free:   0.232
Authors: S.Bouyain
Key ref:
S.Bouyain and D.J.Watkins (2010). The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules. Proc Natl Acad Sci U S A, 107, 2443-2448. PubMed id: 20133774 DOI: 10.1073/pnas.0911235107
07-Nov-09     Release date:   22-Dec-09    
Go to PROCHECK summary

Protein chain
No UniProt id for this chain
Struc: 376 a.a.
Protein chain
Pfam   ArchSchema ?
Q05909  (PTPRG_MOUSE) -  Receptor-type tyrosine-protein phosphatase gamma
1442 a.a.
262 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chain B: E.C.  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
+ H(2)O
protein tyrosine
Bound ligand (Het Group name = NAG)
matches with 47.62% similarity
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site


DOI no: 10.1073/pnas.0911235107 Proc Natl Acad Sci U S A 107:2443-2448 (2010)
PubMed id: 20133774  
The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules.
S.Bouyain, D.J.Watkins.
The receptor protein tyrosine phosphatases gamma (PTPRG) and zeta (PTPRZ) are expressed primarily in the nervous system and mediate cell adhesion and signaling events during development. We report here the crystal structures of the carbonic anhydrase-like domains of PTPRZ and PTPRG and show that these domains interact directly with the second and third immunoglobulin repeats of the members of the contactin (CNTN) family of neural recognition molecules. Interestingly, these receptors exhibit distinct specificities: PTPRZ binds only to CNTN1, whereas PTPRG interacts with CNTN3, 4, 5, and 6. Furthermore, we present crystal structures of the four N-terminal immunoglobulin repeats of mouse CNTN4 both alone and in complex with the carbonic anhydrase-like domain of mouse PTPRG. In these structures, the N-terminal region of CNTN4 adopts a horseshoe-like conformation found also in CNTN2 and most likely in all CNTNs. This restrained conformation of the second and third immunoglobulin domains creates a binding site that is conserved among CNTN3, 4, 5, and 6. This site contacts a discrete region of PTPRG composed primarily of an extended beta-hairpin loop found in both PTPRG and PTPRZ. Overall, these findings implicate PTPRG, PTPRZ and CNTNs as a group of receptors and ligands involved in the manifold recognition events that underlie the construction of neural networks.
  Selected figure(s)  
Figure 4.
Structure of mouse CNTN4^Ig1-4. (A) Ribbon diagram of mouse CNTN4^Ig1-4. The letters N and C indicate the N- and C-termini, respectively. Disulfide bonds are shown as orange ball-and-stick models. Asparagine-linked N-acetylglucosamine residues are depicted as gray ball-and-stick models along with the asparagine side chain. Ig domains 1, 2, 3, and 4 are colored cyan, green, gold, and red, respectively. (B) Stereo view of the interface between Ig domains 2 and 3 in CNTN4^Ig1-4. Residues at the interface between the two domains are shown as ball-and-sticks with transparent spheres (gray) and colored green (Ig2) or gold (Ig3).
Figure 6.
Stereo view of the PTPRG^CA·CNTN4^Ig1-4 interface. This view is in the same orientation as the right view in Fig. 5. Residues are shown as ball-and-sticks with transparent gray spheres for those involved in van der Waals contacts. Dashed lines indicate potential hydrogen bonds and salt bridges. Residues from CNTN4^Ig2, CNTN4^Ig3, and PTPRG^CA are colored green, gold, and magenta, respectively.
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21402080 B.H.Biersmith, M.Hammel, E.R.Geisbrecht, and S.Bouyain (2011).
The immunoglobulin-like domains 1 and 2 of the protein tyrosine phosphatase LAR adopt an unusual horseshoe-like conformation.
  J Mol Biol, 408, 616-627.
PDB codes: 3pxh 3pxj
  20714415 S.Bouyain, and D.J.Watkins (2010).
Identification of tyrosine phosphatase ligands for contactin cell adhesion molecules.
  Commun Integr Biol, 3, 284-286.  
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