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PDBsum entry 3plf

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protein ligands metals Protein-protein interface(s) links
Protein binding/ligase PDB id
3plf
Jmol
Contents
Protein chains
301 a.a. *
Ligands
ARG-PTR-ASP-ALA ×2
Metals
_CL ×4
_CA ×2
Waters ×584
* Residue conservation analysis
PDB id:
3plf
Name: Protein binding/ligase
Title: Reverse binding mode of metrd peptide complexed with c-cbl t
Structure: Metrd peptide. Chain: a, c. Engineered: yes. E3 ubiquitin-protein ligase cbl. Chain: b, d. Fragment: tkb domain. Synonym: casitas b-lineage lymphoma proto-oncogene, proto-o cbl, ring finger protein 55, signal transduction protein cb engineered: yes
Source: Synthetic: yes. Other_details: this is a designed peptide (two residues swi position) based on human met protein sequence.. Homo sapiens. Human. Organism_taxid: 9606. Gene: c-cbl. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.92Å     R-factor:   0.160     R-free:   0.180
Authors: Q.Sun,J.Sivaraman
Key ref: Q.Sun et al. (2011). An adjacent arginine, and the phosphorylated tyrosine in the c-Met receptor target sequence, dictates the orientation of c-Cbl binding. FEBS Lett, 585, 281-285. PubMed id: 21163258
Date:
15-Nov-10     Release date:   01-Dec-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P22681  (CBL_HUMAN) -  E3 ubiquitin-protein ligase CBL
Seq:
Struc:
 
Seq:
Struc:
906 a.a.
301 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     regulation of signaling   2 terms 
  Biochemical function     signal transducer activity     4 terms  

 

 
FEBS Lett 585:281-285 (2011)
PubMed id: 21163258  
 
 
An adjacent arginine, and the phosphorylated tyrosine in the c-Met receptor target sequence, dictates the orientation of c-Cbl binding.
Q.Sun, C.Ng, G.R.Guy, J.Sivaraman.
 
  ABSTRACT  
 
Previously, we have demonstrated that the tyrosine phosphorylated hepatocyte growth factor receptor (Met) binds to the c-Cbl phosphotyrosine-recognition, tyrosine kinase binding (TKB) domain in a reverse orientation compared to other c-Cbl binding partners. A Met peptide with the DpYR motif changed to RpYD (MetRD) retains a similar TKB binding affinity as the native Met peptide. However, the TKB: MetRD complex crystal structure reveals a complete reversal of the binding orientation. Collated data indicates that both binding and orientation is dictated by the phosphorylated tyrosine and an adjacent arginine forming intra-peptide hydrogen bonds and aligning unidirectionally with complementary charges in the phosphotyrosine binding pocket of c-Cbl.