Document 0083
 DOCN  M9480083
 TI    Crystallization and preliminary X-ray analysis of GAP 31. A protein
       which inhibits the life cycle of HIV-1.
 DT    9410
 AU    Lee-Huang S; Kung HF; Chen HC; Huang PL; Rybak SM; Huang PL; Bourinbaiar
       AS; Musayev F; Liaw YC; Department of Biochemistry, New York University
       School of; Medicine, NY 10016.
 SO    J Mol Biol. 1994 Jul 1;240(1):92-4. Unique Identifier : AIDSLINE
       MED/94293324
 AB    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%.
 DE    Antiviral Agents/*CHEMISTRY/ISOLATION & PURIF/TOXICITY  Crystallization
       Crystallography, X-Ray/METHODS  HIV-1/*DRUG EFFECTS/PHYSIOLOGY  Plant
       Proteins/*CHEMISTRY/ISOLATION & PURIF/*TOXICITY  *Protein Conformation
       Support, Non-U.S. Gov't  Support, U.S. Gov't, P.H.S.  Virus
       Replication/DRUG EFFECTS  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).