[HTML][HTML] Replacing a lectin domain residue in L-selectin enhances binding to P-selectin glycoprotein ligand-1 but not to 6-sulfo-sialyl Lewis x
AG Klopocki, T Yago, P Mehta, J Yang, T Wu… - Journal of biological …, 2008 - ASBMB
Selectin-ligand interactions (bonds) mediate leukocyte rolling on vascular surfaces. The
molecular basis for differential ligand recognition by selectins is poorly understood. Here, we
show that substituting one residue (A108H) in the lectin domain of L-selectin increased its
force-free affinity for a glycosulfopeptide binding site (2-GSP-6) on P-selectin glycoprotein
ligand-1 (PSGL-1) but not for a sulfated-glycan binding site (6-sulfo-sialyl Lewis x) on
peripheral node addressin. The increased affinity of L-selectinA108H for 2-GSP-6 was due …
molecular basis for differential ligand recognition by selectins is poorly understood. Here, we
show that substituting one residue (A108H) in the lectin domain of L-selectin increased its
force-free affinity for a glycosulfopeptide binding site (2-GSP-6) on P-selectin glycoprotein
ligand-1 (PSGL-1) but not for a sulfated-glycan binding site (6-sulfo-sialyl Lewis x) on
peripheral node addressin. The increased affinity of L-selectinA108H for 2-GSP-6 was due …
