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PDBsum entry 4eyn

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protein metals Protein-protein interface(s) links
Hormone PDB id
4eyn
Jmol
Contents
Protein chains
21 a.a.
30 a.a.
Metals
_CL ×2
_ZN ×2
Waters ×125
PDB id:
4eyn
Name: Hormone
Title: Human insulin
Structure: Insulin a chain. Chain: a, c. Fragment: unp residues 90-110. Insulin b chain. Chain: b, d. Fragment: unp residues 25-54
Source: Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606
Resolution:
1.53Å     R-factor:   0.178     R-free:   0.271
Authors: M.P.Favero-Retto,L.C.Palmieri,L.M.T.R.Lima
Key ref: M.P.Fávero-Retto et al. (2013). Structural meta-analysis of regular human insulin in pharmaceutical formulations. Eur J Pharm Biopharm, 85, 1112-1121. PubMed id: 23692694 DOI: 10.1016/j.ejpb.2013.05.005
Date:
01-May-12     Release date:   01-May-13    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
Seq:
Struc:
110 a.a.
21 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  

 

 
DOI no: 10.1016/j.ejpb.2013.05.005 Eur J Pharm Biopharm 85:1112-1121 (2013)
PubMed id: 23692694  
 
 
Structural meta-analysis of regular human insulin in pharmaceutical formulations.
M.P.Fávero-Retto, L.C.Palmieri, T.A.Souza, F.C.Almeida, L.M.Lima.
 
  ABSTRACT  
 
We have studied regular acting, wild-type human insulin at potency of 100U/mL from four different pharmaceutical products directly from their final finished formulation by the combined use of mass spectrometry (MS), dynamic light scattering (DLS), small-angle X-ray scattering (SAXS), nuclear magnetic resonance (NMR), and single-crystal protein crystallography (PX). All products showed similar oligomeric assembly in solution as judged by DLS and SAXS measurements. The NMR spectra were compatible with well folded proteins, showing close conformational identity for the human insulin in the four products. Crystallographic assays conducted with the final formulated products resulted in all insulin crystals belonging to the R3 space group with two a dimer in the asymmetric unit, both with the B-chain in the T configuration. Meta-analysis of the 24 crystal structures solved from the four distinct insulin products revealed close similarity between them regardless of variables such as biological origin, product batch, country origin of the product, and analytical approach, revealing a low conformational variability for the converging insulin structural ensemble. We propose the use of MS, SAXS, NMR fingerprint, and PX as a precise chemical and structural proof of folding identity of regular insulin in the final, formulated product.