TY  - JOUR
AU  - Weiergräber, Oliver H.
AU  - Petrović, Dušan
AU  - Kislat, Andreas
AU  - Pattky, Martin
AU  - Fabig, Judith
AU  - Batra-Safferling, Renu
AU  - Schulte am Esch, Jan
AU  - Hänel, Karen
AU  - Huhn, Carolin
AU  - Strodel, Birgit
AU  - Homey, Bernhard
AU  - Willbold, Dieter
TI  - Structure and Dynamics of Human Chemokine CCL16—Implications for Biological Activity
JO  - Biomolecules
VL  - 12
IS  - 11
SN  - 2218-273X
CY  - Basel
PB  - MDPI
M1  - FZJ-2022-04909
SP  - 1588 -
PY  - 2022
AB  - Human C-C motif ligand 16 (CCL16) is a chemokine that is distinguished by a large cleavable C-terminal extension of unknown significance. Conflicting data have been reported concerning its tissue distribution and modulation of expression, rendering the biological function of CCL16 enigmatic. Here, we report an integrated approach to the characterisation of this chemokine, including a re-assessment of its expression characteristics as well as a biophysical investigation with respect to its structure and dynamics. Our data indicate that CCL16 is chiefly synthesised by hepatocytes, without an appreciable response to mediators of inflammation, and circulates in the blood as a full-length protein. While the crystal structure of CCL16 confirms the presence of a canonical chemokine domain, molecular dynamics simulations support the view that the C-terminal extension impairs the accessibility of the glycosaminoglycan binding sites and may thus serve as an intrinsic modulator of biological activity.
LB  - PUB:(DE-HGF)16
C6  - 36358937
UR  - <Go to ISI:>//WOS:000880888200001
DO  - DOI:10.3390/biom12111588
UR  - https://juser.fz-juelich.de/record/911654
ER  -