Crosslinking-guided Geometry of a Complete CXC Receptor-chemokine Complex and the Basis of Chemokine Subfamily Selectivity

April 13, 2020 | Biology

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No need to search high and low for the latest Biology industry news as Lab.Equipment guarantees you are updated whenever and wherever. This week’s article comes from PLOS Biology:

by Tony Ngo, Bryan S. Stephens, Martin Gustavsson, Lauren G. Holden, Ruben Abagyan, Tracy M. Handel, Irina Kufareva

Chemokines and their receptors are orchestrators of cell migration in humans. Because dysregulation of the receptor-chemokine system leads to inflammation and cancer, both chemokines and receptors are highly sought therapeutic targets. Yet one of the barriers for their therapeutic targeting is the limited understanding of the structural principles behind receptor-chemokine recognition and selectivity. The existing structures do not include CXC subfamily complexes and lack information about the receptor distal N-termini, despite the importance of the latter in signaling, regulation, and bias. Here, we report the discovery of the geometry of the complex between full-length CXCR4, a prototypical CXC receptor and driver of cancer metastasis, and its endogenous ligand CXCL12. By comprehensive disulfide cross-linking, we establish the existence and the structure of a nov... Find the complete article at the PLOS Biology Blog.

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