Crystallization and preliminary X-ray analysis of GAP 31. A protein which inhibits the life cycle of HIV-1.
GAP 31 is an anti-HIV plant protein that we have identified and purified to homogeneity from Gelonium multiflorum. It is the first reported example of an anti-HIV agent capable of acting against multiple stages of the viral life cycle, on viral infection and viral replication. GAP 31 is a unique paragon of multi-functional protein. In addition to anti-HIV activity, it also exhibits anti-tumor action, DNA binding, RNA binding and ribosome inactivation. The present crystals diffract up to 2.0 A resolution and belong to monoclinic space group P2(1). The cell dimensions are a = 49.30(2) A, b = 44.57(2) A, c = 137.78(7) A and beta = 98.32(3) degrees. There are two molecules of molecular weight 31 kDa in an asymmetric unit with a solvent content of 49%.
Department of Biochemistry, New York University School of Medicine, NY 10016.
S
S
Lee-Huang
H F
HF
Kung
H C
HC
Chen
P L
PL
Huang
S M
SM
Rybak
P L
PL
Huang
A S
AS
Bourinbaiar
F
F
Musayev
Y C
YC
Liaw
D000998:Antiviral Agents / Q000737:chemistry* / Q000302:isolation & purification / Q000633:toxicity; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D015497:HIV-1 / Q000187:drug effects* / Q000502:physiology; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000633:toxicity*; D011487:Protein Conformation; D054789:Ribosome Inactivating Proteins, Type 1; D014779:Virus Replication / Q000187:drug effects
D000998:Antiviral Agents; C071380:GAP31 protein, Gelonium multiflorum; D010940:Plant Proteins; D054789:Ribosome Inactivating Proteins, Type 1