Crystallization and preliminary X-ray analysis of Na-ASP-1, a multi-domain pathogenesis-related-1 protein from the human hookworm parasite Necator americanus.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 61(Pt 4): 391-4, 2005 Apr 01.
Article
em En
| MEDLINE
| ID: mdl-16511050
ABSTRACT
Human hookworm infection is a major cause of anemia and malnutrition in the developing world. In an effort to control hookworm infection, the Human Hookworm Vaccine Initiative has identified candidate vaccine antigens from the infective larval stage (L3) of the parasite, including a family of pathogenesis-related-1 (PR-1) proteins known as the ancylostoma-secreted proteins (ASPs). The functions of the ASPs are unknown. In addition, it is unclear why some ASPs have one while others have multiple PR-1 domains. There are no known structures of a multi-domain ASP and in an effort to remedy this situation, recombinant Na-ASP-1 has been expressed, purified and crystallized. Na-ASP-1 is a 406-amino-acid multi-domain ASP from the prevalent human hookworm parasite Necator americanus. Useful X-ray data to 2.2 A have been collected from a crystal that belongs to the monoclinic space group P2(1) with unit-cell parameters a = 67.7, b = 74.27, c = 84.60 A, beta = 112.12 degrees. An initial molecular-replacement solution has been obtained with one monomer in the asymmetric unit.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Necator americanus
/
Antígenos de Helmintos
Tipo de estudo:
Etiology_studies
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2005
Tipo de documento:
Article
País de afiliação:
Estados Unidos