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PDBsum entry 4f1j
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Cell adhesion
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PDB id
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4f1j
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References listed in PDB file
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Key reference
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Title
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Structure of plasmodium falciparum trap (thrombospondin-Related anonymous protein) a domain highlights distinct features in apicomplexan von willebrand factor a homologues.
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Authors
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T.Pihlajamaa,
T.Kajander,
J.Knuuti,
K.Horkka,
A.Sharma,
P.Permi.
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Ref.
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Biochem J, 2013,
450,
469-476.
[DOI no: ]
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PubMed id
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Abstract
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TRAP (thrombospondin-related anonymous protein), localized in the micronemes and
on the surface of sporozoites of the notorious malaria parasite Plasmodium, is a
key molecule upon infection of mammalian host hepatocytes and invasion of
mosquito salivary glands. TRAP contains two adhesive domains responsible for
host cell recognition and invasion, and is known to be essential for
infectivity. In the present paper, we report high-resolution crystal structures
of the A domain of Plasmodium falciparum TRAP with and without bound Mg2+. The
structure reveals a vWA (von Willebrand factor A)-like fold and a functional
MIDAS (metal-ion-dependent adhesion site), as well as a potential heparan
sulfate-binding site. Site-directed mutagenesis and cell-attachment assays were
used to investigate the functional roles of the surface epitopes discovered. The
reported structures are the first determined for a complete vWA domain of
parasitic origin, highlighting unique features among homologous domains from
other proteins characterized hitherto. Some of these are conserved among
Plasmodiae exclusively, whereas others may be common to apicomplexan organisms
in general.
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