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Crystallization and preliminary X-ray analysis of GAP 31. A protein which inhibits the life cycle of HIV-1.
- Source :
-
Journal of molecular biology [J Mol Biol] 1994 Jul 01; Vol. 240 (1), pp. 92-4. - Publication Year :
- 1994
-
Abstract
- 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%.
- Subjects :
- Antiviral Agents isolation & purification
Antiviral Agents toxicity
Crystallization
Crystallography, X-Ray methods
HIV-1 physiology
Plant Proteins isolation & purification
Ribosome Inactivating Proteins, Type 1
Virus Replication drug effects
Antiviral Agents chemistry
HIV-1 drug effects
Plant Proteins chemistry
Plant Proteins toxicity
Protein Conformation
Subjects
Details
- Language :
- English
- ISSN :
- 0022-2836
- Volume :
- 240
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Journal of molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 8021945
- Full Text :
- https://doi.org/10.1006/jmbi.1994.1421