PDBsum entry 1htv

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protein metals Protein-protein interface(s) links
Hormone/growth factor PDB id
Protein chains
(+ 0 more) 21 a.a.
(+ 0 more) 27 a.a.
Waters ×171
PDB id:
Name: Hormone/growth factor
Title: Crystal structure of destripeptide (b28-b30) insulin
Structure: Insulin. Chain: a, c, e, g, i, k. Fragment: insulin a chain. Synonym: destripeptide insulin (dtri). Engineered: yes. Insulin. Chain: b, d, f, h, j, l. Fragment: insulin b chain. Synonym: destripeptide insulin (dtri).
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
Biol. unit: Dodecamer (from PQS)
1.90Å     R-factor:   0.196     R-free:   0.240
Authors: J.Ye,W.Chang,D.Liang
Key ref: J.Ye et al. (2001). Crystal structure of destripeptide (B28-B30) insulin: implications for insulin dissociation. Biochim Biophys Acta, 1547, 18-25. PubMed id: 11343787 DOI: 10.1016/S0167-4838(01)00160-1
01-Jan-01     Release date:   23-May-01    
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Protein chains
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
110 a.a.
21 a.a.
Protein chains
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
110 a.a.
27 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/S0167-4838(01)00160-1 Biochim Biophys Acta 1547:18-25 (2001)
PubMed id: 11343787  
Crystal structure of destripeptide (B28-B30) insulin: implications for insulin dissociation.
J.Ye, W.Chang, D.Liang.
Destripeptide (B28-B30) insulin (DTRI) is an insulin analogue that has much weaker association ability than native insulin but keeps most of its biological activity. It can be crystallized from a solution containing zinc ions at near-neutral pH. Its crystal structure has been determined by molecular replacement and refined at 1.9 A resolution. DTRI in the crystal exists as a loose hexamer compared with 2Zn insulin. The hexamer only contains one zinc ion that coordinates to the B10 His residues of three monomers. Although residues B28-B30 are located in the monomer-monomer interface within a dimer, the removal of them can simultaneously weaken both the interactions between monomers within the dimer and the interactions between dimers. Because the B-chain C-terminus of insulin is very flexible, we take the DTRI hexamer as a transition state in the native insulin dissociation process and suggest a possible dissociation process of the insulin hexamer based on the DTRI structure.

Literature references that cite this PDB file's key reference

  PubMed id Reference
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.  
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