Crystals and a low resolution structure of interleukin-2

Recombinant derived human interleukin-2 and an analog in which cysteine 125 has been replaced with alanine have been crystallized in a form suitable for x-ray diffraction. The crystals are triclinic, space group P1, with two protein molecules in the unit cell; unit cell parameters are a = 55.8 A, b...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1987-09, Vol.262 (25), p.12306-12308
Main Authors: Brandhuber, B J, Boone, T, Kenney, W C, McKay, D B
Format: Article
Language:English
Subjects:
Analysis of the immune response. Humoral and cellular immunity
Biological and medical sciences
Crystallization
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Humans
Immunobiology
Interleukin-2
Lymphokines, interleukins ( function, expression)
Mathematics
Models, Structural
Recombinant Proteins
Regulatory factors and their cellular receptors
X-Ray Diffraction
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Recombinant derived human interleukin-2 and an analog in which cysteine 125 has been replaced with alanine have been crystallized in a form suitable for x-ray diffraction. The crystals are triclinic, space group P1, with two protein molecules in the unit cell; unit cell parameters are a = 55.8 A, b = 40.1 A, c = 33.7 A, alpha = 90.0 degrees, beta = 109.3 degrees, gamma = 93.2 degrees. The interleukin-2 structure has been solved to 5.5 A resolution using heavy atom isomorphous replacement methods. The resultant low resolution model reveals a significant fraction of alpha helical secondary structure and outlines the overall tertiary structure of the molecule.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)45352-5