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PDBsum entry 2omg

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protein ligands metals Protein-protein interface(s) links
Hormone PDB id
2omg
Jmol
Contents
Protein chains
21 a.a.
28 a.a. *
Ligands
CRS ×3
URE ×6
ARF ×5
Metals
_NA
_ZN
_CL
Waters ×99
* Residue conservation analysis
PDB id:
2omg
Name: Hormone
Title: Structure of human insulin cocrystallized with protamine and
Structure: Insulin a chain. Chain: a, c, e. Insulin b chain. Chain: b, d, f
Source: Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606
Resolution:
1.52Å     R-factor:   0.184     R-free:   0.209
Authors: M.Norrman,G.Schluckebier
Key ref: M.Norrman et al. (2007). Structural characterization of insulin NPH formulations. Eur J Pharm Sci, 30, 414-423. PubMed id: 17339105
Date:
22-Jan-07     Release date:   27-Mar-07    
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.
28 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  

 

 
Eur J Pharm Sci 30:414-423 (2007)
PubMed id: 17339105  
 
 
Structural characterization of insulin NPH formulations.
M.Norrman, F.Hubálek, G.Schluckebier.
 
  ABSTRACT  
 
Insulin NPH (neutral protamine hagedorn) has for long been one of the most important therapeutic formulations for the treatment of diabetes. The protracted action profile of NPH formulations is gained from crystallizing insulin with zinc in the presence of the basic poly-arginine peptide protamine. In spite of its long history and successful use, the binding mode of the insulin-protamine complex is not known. In this study, three different systems were used to study protamine binding to insulin. In the first system, crystals of an insulin-protamine complex grown in the presence of urea and diffracting to 1.5A resolution were analyzed. In the second system, a shorter peptide consisting of 12 arginine residues was co-crystallized with insulin in order to reduce the flexibility and thereby improve the electron density of the peptide. Both systems yielded data to a significantly higher resolution than obtained previously. In addition, a third system was analyzed where crystals of insulin and protamine were grown in the absence of urea, with conditions closely resembling the pharmaceutical formulation. Data from these NPH microcrystals could for the first time be collected to 2.2A resolution at a micro focused X-ray beamline. Analysis of all three crystal forms reveal potential protamine density located close to the solvent channel leading to the centrally located zinc atoms in the insulin hexamer and support that protamine binds to insulin in a not well defined conformation.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18391409 R.Sanishvili, V.Nagarajan, D.Yoder, M.Becker, S.Xu, S.Corcoran, D.L.Akey, J.L.Smith, and R.F.Fischetti (2008).
A 7 microm mini-beam improves diffraction data from small or imperfect crystals of macromolecules.
  Acta Crystallogr D Biol Crystallogr, 64, 425-435.  
18757876 Y.Bromberg, G.Yachdav, and B.Rost (2008).
SNAP predicts effect of mutations on protein function.
  Bioinformatics, 24, 2397-2398.  
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