Structural highlights
Publication Abstract from PubMed
The crystal structure of the catalytic domain of the ADP ribosylation factor GTPase-activating protein (ARFGAP) from Plasmodium falciparum has been determined and refined to 2.4 A resolution. Multiwavength anomalous diffraction (MAD) data were collected utilizing the Zn(2+) ion bound at the zinc-finger domain and were used to solve the structure. The overall structure of the domain is similar to those of mammalian ARFGAPs. However, several amino-acid residues in the area where GAP interacts with ARF1 differ in P. falciparum ARFGAP. Moreover, a number of residues that form the dimer interface in the crystal structure are unique in P. falciparum ARFGAP.
Structure of the catalytic domain of Plasmodium falciparum ARF GTPase-activating protein (ARFGAP).,Cook WJ, Senkovich O, Chattopadhyay D Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt 11):1339-44., Epub 2011 Oct 25. PMID:22102228[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cook WJ, Senkovich O, Chattopadhyay D. Structure of the catalytic domain of Plasmodium falciparum ARF GTPase-activating protein (ARFGAP). Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt 11):1339-44., Epub 2011 Oct 25. PMID:22102228 doi:10.1107/S1744309111032507
