Three-dimensional structure of a genetically engineered variant of porcine growth hormone

The three-dimensional structure of a genetically engineered variant of porcine growth hormone, methionyl porcine somatotropin (MPS), has been determined at 2.8- angstrom resolution, using single crystal x-ray diffraction techniques. Phases were obtained by use of a single isomorphous K2OsCl6 derivat...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1987-09, Vol.84 (18), p.6434-6437
Main Authors: Abdel-Meguid, S.S, Shieh, H.S, Smith, W.W, Dayringer, H.E, Violand, B.N, Bentle, L.A
Format: Article
Language:English
Subjects:
ACIDE AMINE
Amino Acid Sequence
AMINO ACIDS
AMINOACIDOS
Animals
Biological and medical sciences
CERDO
CHEMISTRY
CHIMIE
Computer Simulation
Connectivity
CRYSTALLOGRAPHY
Crystals
Cytochrome b Group
Cytochrome c Group
Cytochromes
Escherichia coli Proteins
Fundamental and applied biological sciences. Psychology
GENETIC ENGINEERING
GENIE GENETIQUE
Growth Hormone
Growth hormones
Hemerythrin - analogs & derivatives
HORMONAS PITUITARIAS
HORMONE HYPOPHYSAIRE
Hormones
INGENIERIA GENETICA
Molecular biophysics
Molecules
pigs
PITUITARY HORMONES
PORCIN
Protein Conformation
Proteins
QUIMICA
Recombinant Proteins
Structure in molecular biology
SWINE
tertiary structure
Tridimensional structure
X-ray crystallography
X-Ray Diffraction
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Description
Summary:The three-dimensional structure of a genetically engineered variant of porcine growth hormone, methionyl porcine somatotropin (MPS), has been determined at 2.8- angstrom resolution, using single crystal x-ray diffraction techniques. Phases were obtained by use of a single isomorphous K2OsCl6 derivative and were improved by use of the density modification procedure. The MPS structure is predominantly helical. It consists mainly of four antiparallel α -helices arranged in a left twisted helical bundle, a structural motif observed in a number of other unrelated proteins. However, the way the four helices are connected in the bundle is unusual and, to our knowledge, has never been reported before. Alignment of the amino acid sequence of MPS with that of other growth hormones reveals that residues within the α -helices are predominantly invariant and thus these invariant residues are necessary to maintain the structural integrity of these proteins.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.84.18.6434