Structure-guided design of sialic acid-based Siglec inhibitors and crystallographic analysis in complex with sialoadhesin (Q27641193)

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Katsumi Maenaka

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Taeko Maenaka

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Reinhard Brossmer

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Sørge Kelm

Siglecs, sialic acids and innate immunity

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publication date

May 2003

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557-67

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P75 interacts with the Nogo receptor as a co-receptor for Nogo, MAG and OMgp

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Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily

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A small region of the natural killer cell receptor, Siglec-7, is responsible for its preferred binding to alpha 2,8-disialyl and branched alpha 2,6-sialyl residues. A comparison with Siglec-9.

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The amino-terminal immunoglobulin-like domain of sialoadhesin contains the sialic acid binding site. Comparison with CD22.

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Crystal structure of the N-terminal domain of sialoadhesin in complex with 3' sialyllactose at 1.85 A resolution

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High resolution crystal structures of Siglec-7. Insights into ligand specificity in the Siglec family

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Myelin-associated glycoprotein interacts with neurons via a sialic acid binding site at ARG118 and a distinct neurite inhibition site

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Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1

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