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PDBsum entry 2v70
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Structural protein
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PDB id
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2v70
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References listed in PDB file
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Key reference
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Title
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Production of slit2 lrr domains in mammalian cells for structural studies and the structure of human slit2 domain 3.
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Authors
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C.Morlot,
W.Hemrika,
R.A.Romijn,
P.Gros,
S.Cusack,
A.A.Mccarthy.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2007,
63,
961-968.
[DOI no: ]
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PubMed id
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Abstract
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Slit2 and Roundabout 1 (Robo1) provide a key ligand-receptor interaction for the
navigation of commissural neurons during the development of the central nervous
system. Slit2 is a large multidomain protein containing an unusual domain
organization of four tandem leucine-rich repeat (LRR) domains at its N-terminus.
These domains are well known to mediate protein-protein interactions; indeed,
the Robo1-binding region has been mapped to the concave face of the second LRR
domain. It has also been shown that the fourth LRR domain may mediate Slit
dimerization and that both the first and second domains can bind heparin. Thus,
while roles have been ascribed for three of the LRR domains, there is still no
known role for the third domain. Each of the four LRR domains from human Slit2
have now been successfully expressed in milligram quantities using expression in
mammalian cells. Here, the crystallization of the second and third LRR domains
and the structure of the third LRR domain are presented. This is the first
structure of an LRR domain from human Slit2, which has an extra repeat compared
with the Drosophila homologue. It is proposed that a highly conserved patch of
surface residues on the concave face may mediate any protein-protein
interactions involving this LRR domain, a result that will be useful in guiding
further studies on Slit2.
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Figure 2.
Figure 2 Structure of Slit2 LRR domains. The N- and C-terminal
capping domains are shown in purple and blue, respectively, and
the LRR repeats are coloured orange. The disulfide bridges are
drawn in yellow ball-and-stick representation and the
N-acetylglucosamine is drawn in green stick representation. (a,
b) Ribbon diagram of human Slit2 D3 in two orthogonal
orientations. (c) Ribbon diagram of Drosophila Slit D3.
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Figure 4.
Figure 4 The sequence conservation of surface residues was
mapped onto Slit2 D3 and is indicated with a colour gradient
from dark green (most conserved) to white (most divergent) in
two orientations. (a) Concave face in an orientation identical
to Fig. 2-. (b) Convex face showing the N-acetylglucosamine. The
sequence conservation was mapped onto the surface with ConSurf
(Landau et al., 2005[Landau, M., Mayrose, I., Rosenberg, Y.,
Glaser, F., Martz, E., Pupko, T. & Ben-Tal, N. (2005). Nucleic
Acids Res. 33, W299-W302.]).
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2007,
63,
961-968)
copyright 2007.
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