Letter: Insulin activity: the solid matrix.

R W Butcher; O B Crofford; S Gammeltoff; J Gliemann; J R Gavin; I D Goldfine; C R Kahn; M Rodbell; J Roth; L Jarrett; J Larner; R J Lefkowitz; R Levine; G V Marinetti

doi:10.1126/science.182.4110.396-a

PubMed · 4356902

Letter: Insulin activity: the solid matrix.

R W Butcher·O B Crofford·S Gammeltoff·J Gliemann·J R Gavin·I D Goldfine·C R Kahn·M Rodbell·J Roth·L Jarrett·J Larner·R J Lefkowitz·R Levine·G V Marinetti

View original source ↗Export metadata ↓

Abstract

The source did not provide an abstract. Follow the original record for more information.

Explore related subjects

Insulin Polysaccharides Receptors, Cell Surface Journal Article

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

R W Butcher, O B Crofford, S Gammeltoff, J Gliemann, J R Gavin, I D Goldfine, C R Kahn, M Rodbell, J Roth, L Jarrett, J Larner, R J Lefkowitz, R Levine, G V Marinetti. 1973-10-26. Letter: Insulin activity: the solid matrix.. https://doi.org/10.1126/science.182.4110.396-a

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed1992

Structure of a rhombohedral R6 insulin/phenol complex.

Hexameric insulin has been crystallized from different conditions in a variety of crystalline modifications. In the presence of approximately 1% phenol and at a pH of 8.5, a new rhombohedral form is produced, space group R3, a = 79.92A and c = 40.39A, in which the asymmetric unit consists of a dimer. The structure has been solved and refined, using data between 8.0 and 2.5A resolution, to a residual of 0.157. The two monomers in the asymmetric unit have nearly identical R conformations, that is, residues B1 through B8 are alpha-helical, producing a continuous alpha-helix from B1 through B19. A phenol molecule is hydrogen bonded to the carbonyl oxygen of A6 Cys of each monomer. Small differences in conformation and the final (2Fo-Fc) and difference electron density maps suggest that an additional phenol molecule is coordinated to one of the two zinc ions.

Insulin↗

PubMed1992

Flexibility in crystalline insulins.

Comparisons of atomic models for chemically identical protein molecules solved in differing crystal environments provide information on flexibility in the protein structure. The structures of five T4 lysozyme proteins in differing crystal environments showed large relative displacements of the two domains with conserved backbone conformations that are connected by a flexible hinge (H. R. Faber and B. W. Matthews. 1990. Nature (Lond.). 348:263-266). In contrast, my comparison of the positions of all the atoms in two crystal forms of insulin shows that the structural changes caused by the differing crystal contacts are contained within nearby amino acids and are not propagated through the core of the insulin molecule. Groups of atoms that are most significantly displaced are not shifted in large rigid units but are repacked into new and distinct conformations. The transmission of displacements through the single domain insulin molecule is, like the movements due to thermal vibrations (D. L. D. Caspar, J. Clarage, D. M. Salunke, M. S. Clarage. 1988. Nature (Lond.). 332:659-662), characterized by short-range interactions between small atomic groups.

Insulin↗

PubMed1992

Phospholipid content of untreated and insulin treated cells of Neurospora crassa (wall-less strain).

Phosphatidylcholine (51.2%) and phosphatidyl-ethanolamine (38.3%) are the most abundant phospholipids in the wall-less strain of Neurospora crassa. Insulin treatment exerted no change on the amount of phosphoinositides, although some previous results proved the existence of specific insulin receptors and specific effect of insulin on glucose metabolism in these cells. Long (20 h) treatment with insulin also failed to cause biologically significant changes.

Insulin↗