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PDBsum entry 2ceu

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protein ligands Protein-protein interface(s) links
Hormone PDB id
2ceu
Jmol
Contents
Protein chains
21 a.a.
24 a.a.
Ligands
SO4 ×3
Waters ×65
PDB id:
2ceu
Name: Hormone
Title: Despentapeptide insulin in acetic acid (ph 2)
Structure: Insulin. Chain: a, c. Synonym: despentapeptide-b26-b30 insulin. Engineered: yes. Insulin. Chain: b, d. Synonym: despentapeptide-b26-b30 insulin. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932. Expression_system_taxid: 4932
Biol. unit: Tetramer (from PDB file)
Resolution:
1.80Å     R-factor:   0.174     R-free:   0.211
Authors: J.L.Whittingham,Y.Zhang,L.Zakova,E.J.Dodson,J.P.Turkenburg, J.Brange,G.G.Dodson
Key ref:
J.L.Whittingham et al. (2006). I222 crystal form of despentapeptide (B26-B30) insulin provides new insights into the properties of monomeric insulin. Acta Crystallogr D Biol Crystallogr, 62, 505-511. PubMed id: 16627943 DOI: 10.1107/S0907444906006871
Date:
10-Feb-06     Release date:   03-Mar-06    
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.
24 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: 10.1107/S0907444906006871 Acta Crystallogr D Biol Crystallogr 62:505-511 (2006)
PubMed id: 16627943  
 
 
I222 crystal form of despentapeptide (B26-B30) insulin provides new insights into the properties of monomeric insulin.
J.L.Whittingham, Z.Youshang, L.Záková, E.J.Dodson, J.P.Turkenburg, J.Brange, G.G.Dodson.
 
  ABSTRACT  
 
Despentapeptide (des-B26-B30) insulin (DPI), an active modified insulin, has been crystallized in the presence of 20% acetic acid pH 2. A crystal structure analysis to 1.8 A spacing (space group I222) revealed that the DPI molecule, which is unable to make beta-strand interactions for physiological dimer formation and is apparently monomeric in solution, formed an alternative lattice-generated dimer. The formation of this dimer involved interactions between surfaces which included the B9-B19 alpha-helices (usually buried by the dimer-dimer contacts within the native hexamer). The two crystallographically independent molecules within the dimer were essentially identical and were similar in conformation to T-state insulin as seen in the T(6) insulin hexamer. An unusual feature of each molecule in the dimer was the presence of two independent conformations at the B-chain C-terminus (residues B20-B25). Both conformations were different from that of native insulin, involving a 3.5 A displacement of the B20-B23 beta-turn and a repositioning of residue PheB25 such that it made close van der Waals contact with the main body of the molecule, appearing to stabilize the B-chain C-terminus.
 
  Selected figure(s)  
 
Figure 5.
Figure 5 Stereoview ball-and-stick diagram showing the two HSO[4]^- ion-binding sites in the DPI_HAc crystal structure. HSO[4]^- ions are coloured yellow, adjacent DPI_HAc dimers in the crystal are coloured either grey or black with white atoms and water molecules are represented by red spheres. Hydrogen bonds between one of the HSO[4]^- ions and atoms of the A-chain N-terminus are shown as dashed lines. This figure was produced using BobScript (Esnouf, 1997[Esnouf, R. M. (1997). J. Mol. Graph. 15, 132-134.]).
Figure 6.
Figure 6 C^ -trace comparisons of the DPI_HAc molecule (blue) with (a) molecule 1 of T[6] insulin (red), (b) molecule 1 of the low-pH orthorhombic insulin (yellow) and (c) DPI (orange; Bi et al., 1983[Bi, R.-C., Dauter, Z., Dodson, E., Dodson, G., Gordiano, F., Hubbard, R. & Reynolds, C. (1983). Proc. Indian Acad. Sci. (Chem. Sci.), 92, 473-483.]). Molecules were superimposed on the B9-B19 -helices using the CCP4 suite (Collaborative Computational Project, Number 4, 1994[Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.]). This figure was produced using BobScript (Esnouf, 1997[Esnouf, R. M. (1997). J. Mol. Graph. 15, 132-134.]) and Raster3D (Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.]).
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 505-511) copyright 2006.  
  Figures were selected by an automated process.