5AZZ

Crystal structure of seleno-insulin


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.45 Å
  • R-Value Free: 0.192 
  • R-Value Work: 0.168 
  • R-Value Observed: 0.170 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Preparation of Selenoinsulin as a Long-Lasting Insulin Analogue.

Arai, K.Takei, T.Okumura, M.Watanabe, S.Amagai, Y.Asahina, Y.Moroder, L.Hojo, H.Inaba, K.Iwaoka, M.

(2017) Angew Chem Int Ed Engl 56: 5522-5526

  • DOI: https://doi.org/10.1002/anie.201701654
  • Primary Citation of Related Structures:  
    5AZZ

  • PubMed Abstract: 

    Synthetic insulin analogues with a long lifetime are current drug targets for the therapy of diabetic patients. The replacement of the interchain disulfide with a diselenide bridge, which is more resistant to reduction and internal bond rotation, can enhance the lifetime of insulin in the presence of the insulin-degrading enzyme (IDE) without impairing the hormonal function. The [C7U A ,C7U B ] variant of bovine pancreatic insulin (BPIns) was successfully prepared by using two selenocysteine peptides (i.e., the C7U analogues of A- and B-chains, respectively). In a buffer solution at pH 10 they spontaneously assembled under thermodynamic control to the correct insulin fold. The selenoinsulin (Se-Ins) exhibited a bioactivity comparable to that of BPIns. Interestingly, degradation of Se-Ins with IDE was significantly decelerated (τ 1/2 ≈8 h vs. ≈1 h for BPIns). The lifetime enhancement could be due to both the intrinsic stability of the diselenide bond and local conformational changes induced by the substitution.


  • Organizational Affiliation

    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka-shi, Kanagawa, 259-1292, Japan.


Macromolecules

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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Insulin A chain22Bos taurusMutation(s): 1 
UniProt
Find proteins for P01317 (Bos taurus)
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Go to UniProtKB:  P01317
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP01317
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Insulin B chain31Bos taurusMutation(s): 1 
UniProt
Find proteins for P01317 (Bos taurus)
Explore P01317 
Go to UniProtKB:  P01317
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP01317
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.45 Å
  • R-Value Free: 0.192 
  • R-Value Work: 0.168 
  • R-Value Observed: 0.170 
  • Space Group: I 21 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 77.994α = 90
b = 77.994β = 90
c = 77.994γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XDSdata scaling
SHELXDEphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-05-03
    Type: Initial release
  • Version 1.1: 2017-06-14
    Changes: Database references