Ontology highlight
ABSTRACT:
SUBMITTER: Newby ZE
PROVIDER: S-EPMC2568999 | biostudies-literature | 2008 Jun
REPOSITORIES: biostudies-literature
Newby Zachary E R ZE O'Connell Joseph J Robles-Colmenares Yaneth Y Khademi Shahram S Miercke Larry J LJ Stroud Robert M RM
Nature structural & molecular biology 20080525 6
The 2.05-A resolution structure of the aquaglyceroporin from the malarial parasite Plasmodium falciparum (PfAQP), a protein important in the parasite's life cycle, has been solved. The structure provides key evidence for the basis of water versus glycerol selectivity in aquaporin family members. Unlike its closest homolog of known structure, GlpF, the channel conducts both glycerol and water at high rates, framing the question of what determines high water conductance in aquaporin channels. The ...[more]