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PDBsum entry 4xgo
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Protein binding
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PDB id
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4xgo
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References listed in PDB file
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Key reference
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Title
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Biophysical analysis of anopheles gambiae leucine-Rich repeat proteins apl1a1, Apl1b [corrected] and apl1c and their interaction with lrim1.
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Authors
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M.Williams,
B.J.Summers,
R.H.Baxter.
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Ref.
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Plos One, 2015,
10,
e0118911.
[DOI no: ]
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PubMed id
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Abstract
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Natural infection of Anopheles gambiae by malaria-causing Plasmodium parasites
is significantly influenced by the APL1 genetic locus. The locus contains three
closely related leucine-rich repeat (LRR) genes, APL1A, APL1B and APL1C.
Multiple studies have reported the participation of APL1A-C in the immune
response of A. gambiae to invasion by both rodent and human Plasmodium isolates.
APL1C forms a heterodimer with the related LRR protein LRIM1 via a C-terminal
coiled-coil domain that is also present in APL1A and APL1B. The LRIM1/APL1C
heterodimer protects A. gambiae from infection by binding the complement-like
protein TEP1 to form a stable and active immune complex. Here we report solution
x-ray scatting data for the LRIM1/APL1C heterodimer, the oligomeric state of
LRIM1/APL1 LRR domains in solution and the crystal structure of the APL1B LRR
domain. The LRIM1/APL1C heterodimeric complex has a flexible and extended
structure in solution. In contrast to the APL1A, APL1C and LRIM1 LRR domains,
the APL1B LRR domain is a homodimer. The crystal structure of APL1B-LRR shows
that the homodimer is formed by an N-terminal helix that complements for the
absence of an N-terminal capping motif in APL1B, which is a unique distinction
within the LRIM1/APL1 protein family. Full-length APL1A1 and APL1B form a stable
complex with LRIM1. These results support a model in which APL1A1, APL1B and
APL1C can all form an extended, flexible heterodimer with LRIM1, providing a
repertoire of functional innate immune complexes to protect A. gambiae from a
diverse array of pathogens.
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