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PDBsum entry 2mfr

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protein links
Transferase PDB id
2mfr
Jmol
Contents
Protein chain
57 a.a.
PDB id:
2mfr
Name: Transferase
Title: Solution structure of the transmembrane domain of the insuli in micelles
Structure: Insulin receptor. Chain: a. Fragment: unp residues 940-988. Synonym: ir. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: insr. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: Q.Li,Y.L.Wong,C.Kang
Key ref: Q.Li et al. (2014). Solution structure of the transmembrane domain of the insulin receptor in detergent micelles. Biochim Biophys Acta, 1838, 1313-1321. PubMed id: 24440425 DOI: 10.1016/j.bbamem.2014.01.005
Date:
20-Oct-13     Release date:   02-Apr-14    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P06213  (INSR_HUMAN) -  Insulin receptor
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1382 a.a.
57 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 8 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.7.10.1  - Receptor protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
ATP
+ [protein]-L-tyrosine
= ADP
+ [protein]-L-tyrosine phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/j.bbamem.2014.01.005 Biochim Biophys Acta 1838:1313-1321 (2014)
PubMed id: 24440425  
 
 
Solution structure of the transmembrane domain of the insulin receptor in detergent micelles.
Q.Li, Y.L.Wong, C.Kang.
 
  ABSTRACT  
 
The insulin receptor (IR) binds insulin and plays important roles in glucose homeostasis by regulating the tyrosine kinase activity at its C-terminus. Its transmembrane domain (TMD) is shown to be important for transferring conformational changes induced by insulin across the cell membrane to regulate kinase activity. In this study, a construct IR940-988 containing the TMD was expressed and purified for structural studies. Its solution structure in dodecylphosphocholine (DPC) micelles was determined. The sequence containing residues L962 to Y976 of the TMD of the IR in micelles adopts a well-defined helical structure with a kink formed by glycine and proline residues present at its N-terminus, which might be important for its function. Paramagnetic relaxation enhancement (PRE) and relaxation experimental results suggest that residues following the TMD are flexible and expose to aqueous solution. Although purified IR940-988 in micelles existed mainly as a monomeric form verified by gel filtration and relaxation analysis, cross-linking study suggests that it may form a dimer or oligomers under micelle conditions.