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Allovalency observed by transferred NOE: interactions of sulfated tyrosine residues in the N‐terminal segment of CCR5 with the CCL5 chemokine
Author(s) -
Kessler Naama,
Akabayov Sabine R.,
Moseri Adi,
Cohen Leah S.,
Sakhapov Damir,
Bolton David,
Fridman Brandon,
Kay Lewis E.,
Naider Fred,
Anglister Jacob
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15503
Subject(s) - sulfation , chemistry , ccl5 , chemokine receptor , tyrosine , chemokine , biochemistry , cc chemokine receptors , stereochemistry , receptor , in vitro , cytotoxic t cell , il 2 receptor
Sulfation of tyrosine 10, 14 and 15 in the intrinsically disordered N‐terminal segment of the CCR5 chemokine receptor, considerably increases its binding affinity to the CCL5 chemokine. Chemical shift perturbation analysis and TRNOE measurements indicate that each of these sulfated tyrosines can individually occupy the same binding pocket of CCL5 and in a similar manner, suggesting a binding mechanism involving allovalency.