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protein Protein-protein interface(s) links
Hormone PDB id
1dei
Jmol
Contents
Protein chains
21 a.a.
23 a.a.
Waters ×85
PDB id:
1dei
Name: Hormone
Title: Desheptapeptide (b24-b30) insulin
Structure: Insulin. Chain: a, c. Engineered: yes. Mutation: yes. Other_details: desheptapeptide (b24-b30). Insulin. Chain: b, d. Engineered: yes. Mutation: yes.
Source: Sus scrofa. Pig. Organism_taxid: 9823. Organ: pancreas. Organ: pancreas
Biol. unit: Dimer (from PQS)
Resolution:
1.60Å     R-factor:   0.196     R-free:   0.215
Authors: S.-J.Bao,W.-R.Chang,Z.-L.Wan,J.-P.Zhang,D.-C.Liang
Key ref:
S.J.Bao et al. (1997). Crystal structure of desheptapeptide(B24-B30)insulin at 1.6 A resolution: implications for receptor binding. Proc Natl Acad Sci U S A, 94, 2975-2980. PubMed id: 9096331 DOI: 10.1073/pnas.94.7.2975
Date:
15-May-96     Release date:   16-Jun-97    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P01315  (INS_PIG) -  Insulin
Seq:
Struc: 		108 a.a.
21 a.a.
Protein chains
Pfam   ArchSchema ?
P01315  (INS_PIG) -  Insulin
Seq:
Struc: 		108 a.a.
23 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: 10.1073/pnas.94.7.2975 Proc Natl Acad Sci U S A 94:2975-2980 (1997)
PubMed id: 9096331  
 
 
Crystal structure of desheptapeptide(B24-B30)insulin at 1.6 A resolution: implications for receptor binding.
S.J.Bao, D.L.Xie, J.P.Zhang, W.R.Chang, D.C.Liang.
 
  ABSTRACT  
 
The crystal structure of desheptapeptide (B24-B30) insulin (DHPI), a virtually inactive analog of insulin, was determined at 1.6 A resolution. In the refined structure model, DHPI retains three alpha-helices (A1-A8, A12-A18, and B9-B19) as its structural framework, while great conformational changes occur in the N and C termini of B-chain. The beta-turn, which lies in B20-B30 in insulin and insulin analogs with high potency, no longer exists in DHPI. Relative motion is observed among the three alpha-helices, each as a rigid functional group. In contrast, a region covering B5-B6 and A6-A11 exhibits a relatively stable conformation. We interpret our results as identifying: (i) the importance of beta-turn in determining the receptor-binding potency of insulin and (ii) a leading role of PheB24 in maintaining the beta-turn structure.
 
  Selected figure(s)  
 
Figure 3.
Fig. 3. The overall structure of DHPI. (a) A stereo ribbon diagram of DHPI showing view along the local 2-fold axis near (0,0,Z). (b) Stereo C trace of two DHPI molecules, with every fifth residue^ labeled in each chain. Residues are labeled as in Fig. 1. [This figure was produced using MOLSCRIPT (28). 		Figure 4.
Fig. 4. Contacts of two monomers of DHPI or 2Zn insulin in an asymmetric unit. Molecule 1 of DHPI or 2Zn insulin is shown in boldface^ while molecule 2 is shown in regular type. (a) Contacts through hydrophobic interfaces in two DHPI monomers. The residues involved^ in the hydrophobic interaction are highlighted in boldface lines. A hydrogen bond linking Cys111-O and Arg422-NE is shown with a dotted line. (b) Contacts through -strands of C-terminal B-chains in 2Zn insulin dimer. The hydrogen bonds are shown with dotted lines, with bonding residues labeled. Residues are labeled as in Fig. 1. [This figure was produced using MOLSCRIPT (28).
 
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19618407 G.Le Flem, J.Pecher, V.Le Flem-Bonhomme, A.Withdrawn, J.Rochette, J.P.Pujol, and P.Bogdanowicz (2009).
Human insulin A-chain peptide analog(s) with in vitro biological activity.
  Cell Biochem Funct, 27, 370-377.  
16627943 J.L.Whittingham, Z.Youshang, L.Záková, E.J.Dodson, J.P.Turkenburg, J.Brange, and G.G.Dodson (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.
PDB code: 2ceu
15722444 V.Alexandrov, U.Lehnert, N.Echols, D.Milburn, D.Engelman, and M.Gerstein (2005).
Normal modes for predicting protein motions: a comprehensive database assessment and associated Web tool.
  Protein Sci, 14, 633-643.  
14596591 Z.L.Wan, B.Xu, Y.C.Chu, P.G.Katsoyannis, and M.A.Weiss (2003).
Crystal structure of allo-Ile(A2)-insulin, an inactive chiral analogue: implications for the mechanism of receptor binding.
  Biochemistry, 42, 12770-12783.
PDB codes: 1lw8 1pc1 1q4v
11742127 B.Xu, Q.X.Hua, S.H.Nakagawa, W.Jia, Y.C.Chu, P.G.Katsoyannis, and M.A.Weiss (2002).
A cavity-forming mutation in insulin induces segmental unfolding of a surrounding alpha-helix.
  Protein Sci, 11, 104-116.
PDB code: 1k3m
11123908 S.H.Nakagawa, H.S.Tager, and D.F.Steiner (2000).
Mutational analysis of invariant valine B12 in insulin: implications for receptor binding.
  Biochemistry, 39, 15826-15835.  
20229340 S.Bao, J.Zhang, W.Chang, and D.Liang (1999).
Structure of desheptapeptide (B24-B30) insulin in a new crystal form.
  Sci China C Life Sci, 42, 267-273.  
10489447 Z.P.Yao, Z.H.Zeng, H.M.Li, Y.Zhang, Y.M.Feng, and D.C.Wang (1999).
Structure of an insulin dimer in an orthorhombic crystal: the structure analysis of a human insulin mutant (B9 Ser-->Glu).
  Acta Crystallogr D Biol Crystallogr, 55, 1524-1532.
PDB code: 1b9e
9566117 C.McInnes, and B.D.Sykes (1997).
Growth factor receptors: structure, mechanism, and drug discovery.
  Biopolymers, 43, 339-366.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.