[HTML][HTML] Unique role of the chemokine domain of fractalkine in cell capture: kinetics of receptor dissociation correlate with cell adhesion
CA Haskell, MD Cleary, IF Charo - Journal of Biological Chemistry, 2000 - ASBMB
The chemokine fractalkine (FK) has two structural features that make it unique in the
chemokine family: a CX 3 C motif and an extended carboxyl terminus that anchors it to the
cell surface. This mucin-like stalk or an equivalent spacer is required for FK to mediate the
adhesion of cells expressing its receptor, CX 3 CR1. To determine whether the ability of FK
to act as a cell adhesion molecule is due to the unique presentation of a chemokine domain
on a stalk or to properties of the chemokine domain itself, we created a series of chimeras in …
chemokine family: a CX 3 C motif and an extended carboxyl terminus that anchors it to the
cell surface. This mucin-like stalk or an equivalent spacer is required for FK to mediate the
adhesion of cells expressing its receptor, CX 3 CR1. To determine whether the ability of FK
to act as a cell adhesion molecule is due to the unique presentation of a chemokine domain
on a stalk or to properties of the chemokine domain itself, we created a series of chimeras in …