 |
PDBsum entry 2bve
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Immune system
|
PDB id
|
|
|
|
2bve
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystallographic and in silico analysis of the sialoside-Binding characteristics of the siglec sialoadhesin.
|
|
|
Authors
|
|
N.R.Zaccai,
A.P.May,
R.C.Robinson,
L.D.Burtnick,
P.R.Crocker,
R.Brossmer,
S.Kelm,
E.Y.Jones.
|
|
|
Ref.
|
|
J Mol Biol, 2007,
365,
1469-1479.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The Siglec family of receptors mediates cell-surface interactions through
recognition of sialylated glycoconjugates. Previously reported structures of the
N-terminal domain of the Siglec sialoadhesin (SnD1) in complex with various
sialic acid analogs revealed the structural template for sialic acid binding. To
characterize further the carbohydrate-binding properties, we have determined the
crystal structures of SnD1 in the absence of ligand, and in complex with
2-benzyl-Neu5NPro and 2-benzyl-Neu5NAc. These structures reveal that SnD1
undergoes very few structural changes on ligand binding and detail how two novel
classes of sialic acid analogs bind, one of which unexpectedly can induce Siglec
dimerization. In conjunction with in silico analysis, this set of structures
informs us about the design of putative ligands with enhanced binding affinities
and specificities to different Siglecs, and provides data with which to test the
effectiveness of different computational drug design protocols.
|
|
|
|
|
|
|
|
Figure 1.
Figure 1. Compounds detailed in this study and their rIP
(relative inhibitory potency against 2-Me-Neu5NAc) for
sialoadhesin.
|
|
Figure 3.
|
|
|
|
|
|
The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2007,
365,
1469-1479)
copyright 2007.
|
|
|
|
|
|
|
