PDBsum entry 1sdb

Hormone

PDB id: 1sdb

Contents

Protein chains

21 a.a.

23 a.a.

Waters ×33

PDB id:

1sdb

Name:

Hormone

Title:

Porcine desb1-2 despentapeptide(b26-b30) insulin

Structure:

Desb1-2 despentapeptide (b26-b30) insulin. Chain: a. Desb1-2 despentapeptide (b26-b30) insulin. Chain: b

Source:

Sus scrofa. Pig. Organism_taxid: 9823. Organ: pancreas. Organ: pancreas

Biol. unit:

Dimer (from PQS)

Resolution:

1.65Å R-factor: 0.203 R-free: 0.220

Authors:

D.-C.Liang,J.-S.Diao

Key ref:

J.S.Diao et al. (1997). Structure of monomeric porcine DesB1-B2 despentapeptide (B26-B30) insulin at 1.65 A resolution. Acta Crystallogr D Biol Crystallogr, 53, 507-512. PubMed id: 15299880 DOI: 10.1107/S0907444997004034

Date:

29-Jan-96 Release date: 12-Feb-97

Protein chain

P01315  (INS_PIG) -  Insulin from Sus scrofa

Seq: 108 a.a.

Struc: 21 a.a.

Protein chain

P01315  (INS_PIG) -  Insulin from Sus scrofa

Seq: 108 a.a.

Struc: 23 a.a.

DOI no: 10.1107/S0907444997004034

Acta Crystallogr D Biol Crystallogr 53:507-512 (1997)

PubMed id: 15299880

Structure of monomeric porcine DesB1-B2 despentapeptide (B26-B30) insulin at 1.65 A resolution.

J.S.Diao, Z.L.Wan, W.R.Chang, D.C.Liang.

ABSTRACT

Insulin has a concentration of 10(-8)-10(-11) M in the blood which ensures that it circulates and exerts its physiological functions in vivo as a monomer. The crystal structure of monomeric porcine desB1-B2 despentapeptide (B26-B30) insulin (DesB1-2 DPI) with M(r) = 4934 Da has been determined at 1.65 A resolution using the molecular replacement method. A structural comparison between DesB1-2 DPI and 2Zn insulin reveals that the conformation of DesB1-2 DPI is more similar to molecule I than molecule II of 2Zn insulin. The remarkable conformational difference between B25-Phe in DesB1-2 DPI and B25-Phe in despentapeptide (B26-B30) insulin (DPI) indicates that the residue B25-Phe possesses great flexibility and mobility.

Selected figure(s)

Figure 2.
Fig. 2. Stereoview of residue A19­ Tyr superimposed with the corre­ sponding F o ­F~ map contoured at 2.0o­.

Figure 4.
Fig. 4. Stereoview of the F o ­F~ omit map of residues B23­B25 contoured at 2.0o­.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1997, 53, 507-512) copyright 1997.

Figures were selected by an automated process.