Structure of a Murine Leukemia Virus Receptor-Binding Glycoprotein at 2.0 Angstrom Resolution-Reference-Cited by-同舟云学术

Structure of a Murine Leukemia Virus Receptor-Binding Glycoprotein at 2.0 Angstrom Resolution

Published:1997-09-12 Issue:5332 Volume:277 Page:1662-1666
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Fass Deborah¹²³,Davey Robert A.¹²³,Hamson Christian A.¹²³,Kim Peter S.¹²³,Cunningham James M.¹²³,Berger James M.¹²³

Affiliation:

1. D. Fass and P. S. Kim, Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.

2. R. A. Davey, C. A. Hamson, J. M. Cunningham, Howard Hughes Medical Institute, Division of Hematology, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Room 30, Thorn Building, 20 Shattuck Street, Boston, MA 02115, USA.

3. J. M. Berger, Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.

Abstract

An essential step in retrovirus infection is the binding of the virus to its receptor on a target cell. The structure of the receptor-binding domain of the envelope glycoprotein from Friend murine leukemia virus was determined to 2.0 angstrom resolution by x-ray crystallography. The core of the domain is an antiparallel β sandwich, with two interstrand loops forming a helical subdomain atop the sandwich. The residues in the helical region, but not in the β sandwich, are highly variable among mammalian C-type retroviruses with distinct tropisms, indicating that the helical subdomain determines the receptor specificity of the virus.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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