The ability of cells to migrate in response to chemokine mediated signals, a process known as chemotaxis, is fundamental in the context of inflammation, as in many other physiological processes. Chemokines binding to heparan sulphate ensures their correct positioning within tissues and maintains haptotactic gradients along which cell can migrate directionally. In this survey, some structural aspects of the chemokine-heparan sulphate interface are described, with a focus on CXCL12; alternative splicing of which finely tunes its affinity for glycosaminoglycans, through the generation of an intrinsically disordered peptides, and on recent biochemical observations that shed light on both the fine structure and the general topology of the heparan sulphate domains that chemokines recognize.