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When a chemokine binds to its G protein-coupled receptor one of the consequences of receptor activation is a decrease in the levels of receptor present on the cell surface due to more rapid internalization. The mechanism of GPCR internalization

CXCL12 and its receptor CXCR4 have well known roles in bone marrow homing and  mobilization of hematopoietic stem cells and neutrophils, but inflammatory neutrophil  recruitment is governed by CXCR2 and its

Chemokine CXCL4 key to rare COVID-19 vaccine side effect

Plasma concentrations of inflammatory proteins can serve as biomarkers for cardiovascular disease (CVD). Previous studies had linked the T cell chemokine CXCL10/IP-10 to hypertension and heart failure, but failed to achieve the statistical significance necessary for its use as a biomarker for human disease.

As reported recently in the Wall Street Journal and other publications, the human chemokine CXCL4 (also known as platelet factor 4 or PF4) is the common link between COVID-19 vaccine-induced immune thrombotic thrombocytopenia (VITT) and a more common condition known as heparin-induced thrombocytopenia (HIT). 

A new TiBS Spotlight features the work of Protein Foundry scientists and collaborators on the evolution of a highly unusual chemokine.

A shapeshifting immune system protein called XCL1 evolved from a single-shape ancestor hundreds of millions of years ago. Researchers at the Medical College of Wisconsin discovered the molecular basis for how this happened, in  a study

Using a hybrid modeling approach, Fox generated a model for the chemokine XCL1 in complex with its G protein-coupled receptor XCR1 and identified key interaction sites. Changes within a region of XCL1 that determined its binding energy to XCR1 changed the activity of the receptor and, consequently, cell migration