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PDBsum entry 2qiu

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protein metals Protein-protein interface(s) links
Hormone PDB id
2qiu
Jmol
Contents
Protein chains
22 a.a.
30 a.a. *
Metals
_ZN ×2
Waters ×57
* Residue conservation analysis
PDB id:
2qiu
Name: Hormone
Title: Structure of human arg-insulin
Structure: Insulin. Chain: a, c. Fragment: insulin a chain. Insulin. Chain: b, d. Fragment: insulin b chain
Source: Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606
Resolution:
2.00Å     R-factor:   0.203     R-free:   0.249
Authors: R.Sreekanth,V.Pattabhi,S.S.Rajan
Key ref: R.Sreekanth et al. (2008). Structural interpretation of reduced insulin activity as seen in the crystal structure of human Arg-insulin. Biochimie, 90, 467-473. PubMed id: 18029081
Date:
05-Jul-07     Release date:   26-Feb-08    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
Seq:
Struc:
110 a.a.
22 a.a.
Protein chains
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
Seq:
Struc:
110 a.a.
30 a.a.
Key:    PfamA domain  Secondary structure

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biochemical function     hormone activity     1 term  

 

 
Biochimie 90:467-473 (2008)
PubMed id: 18029081  
 
 
Structural interpretation of reduced insulin activity as seen in the crystal structure of human Arg-insulin.
R.Sreekanth, V.Pattabhi, S.S.Rajan.
 
  ABSTRACT  
 
The N-terminal glycine of the A-chain in insulin is reported to be one of the residues that binds to the insulin receptor. Modifications near this region lead to variations in the biological activity of insulin. One such modification viz., an addition of an arginine at the N-terminal A-chain, was reported to possess two-thirds the activity of native insulin. The crystal structure of 2 zinc human arg (A0) insulin has been elucidated to 2A resolution to understand the mechanism of reduction in insulin activity. A conformational transition from T6 to T3R3(f) and a decrease in the surface accessibility of residues in the so called receptor binding region have been observed. The presence of arginine has also induced distortions in the A chain N-terminal helix. The subtle conformational alterations like decrease in surface accessibility, alterations in the charge surface and changes in the relative orientation of the two helices in the A chain may be responsible for the reduction in activity.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19834685 M.Kouach, B.Desbuquois, and F.Authier (2009).
Endosomal proteolysis of internalised [ArgA0]-human insulin at neutral pH generates the mature insulin peptide in rat liver in vivo.
  Diabetologia, 52, 2621-2632.  
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