Ontology highlight
ABSTRACT:
SUBMITTER: Yang J
PROVIDER: S-EPMC41916 | biostudies-other | 1995 May
REPOSITORIES: biostudies-other
Proceedings of the National Academy of Sciences of the United States of America 19950501 10
The perienteric hemoglobin of the parasitic nematode Ascaris has an exceptionally high affinity for oxygen. It is an octameric protein containing two similar heme-binding domains per subunit, but recombinant constructs expressing a single, monomeric heme-binding domain (domain 1; D1) retain full oxygen avidity. We have solved the crystal structure of D1 at 2.2 A resolution. Analysis of the structure reveals a characteristic globin fold and illuminates molecular features involved in oxygen avidit ...[more]