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PDBsum entry 2o6q
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Immune system
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PDB id
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2o6q
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References listed in PDB file
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Key reference
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Title
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Structural diversity of the hagfish variable lymphocyte receptors.
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Authors
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H.M.Kim,
S.C.Oh,
K.J.Lim,
J.Kasamatsu,
J.Y.Heo,
B.S.Park,
H.Lee,
O.J.Yoo,
M.Kasahara,
J.O.Lee.
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Ref.
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J Biol Chem, 2007,
282,
6726-6732.
[DOI no: ]
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PubMed id
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Abstract
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Variable lymphocyte receptors (VLRs) are recently discovered leucine-rich repeat
(LRR) family proteins that mediate adaptive immune responses in jawless fish.
Phylogenetically it is the oldest adaptive immune receptor and the first one
with a non-immunoglobulin fold. We present the crystal structures of one VLR-A
and two VLR-B clones from the inshore hagfish. The hagfish VLRs have the
characteristic horseshoe-shaped structure of LRR family proteins. The backbone
structures of their LRR modules are highly homologous, and the sequence
variation is concentrated on the concave surface of the protein. The
conservation of key residues suggests that our structures are likely to
represent the LRR structures of the entire repertoire of jawless fish VLRs. The
analysis of sequence variability, prediction of protein interaction surfaces,
amino acid composition analysis, and structural comparison with other LRR
proteins suggest that the hypervariable concave surface is the most probable
antigen binding site of the VLR.
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Figure 2.
FIGURE 2. Crystal structure of hagfish VLR-A. A, stereo
view of Eb7VLRA.29. Blue, LRRNT; green, LRR modules; orange,
LRRCT; gray, disulfide bridge; magenta, phenylalanine spine and
asparagine ladder. B, top view of Eb7VLRA.29. This figure was
generated using PyMOL.
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Figure 3.
FIGURE 3. Crystal structure of hagfish VLR-B and structure
alignment of VLR-A and VLR-B. A, stereo view of Eb8VLRB.61.
Blue, LRRNT; green, LRR modules; orange, LRRCT; gray, disulfide
bridge; magenta, phenylalanine spine and asparagine ladder. B,
alignment of the N-terminal half of Eb8VLRB.61 with that of
Eb7VLRA.29. The r.m.s. deviation of the C  positions is 0.55
Å. C, alignment of the C-terminal half of Eb8VLRB.61 with
that of Eb7VLRA.29. The r.m.s. deviation of the C positions is 0.84
Å.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2007,
282,
6726-6732)
copyright 2007.
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