The CXCR4-SDF-1 chemokine receptor complex is involved in both normal and pathological functions in the body, including cancer metastasis.  The CXCR4 receptor is post-translationally modified by tyrosine sulfation at three sites on its N terminus, and this modification is required for binding to the SDF-1 chemokine.  To study the role of tyrosine sulfation in the structure and dynamics of the CXCR4-SDF-1 complex, we conducted molecular dynamics simulations on experimentally determined complexes of CXCR4-SDF-1 that were unsulfated, partially sulfated, and fully sulfated.  A comparison of hydrogen bonding and torsional motions in the simulation trajectories shows that sulfation plays a role in dimer stabilization, and that each additional sulfation site adds to the stability of the dimeric complex.  It is hoped that this work will contribute to therapeutic efforts which target sulfated systems.

Role of tyrosine O-sulfation in the CXCR4-SDF-1 chemokine receptor complex

245th National Meeting (2013)

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