Journal Article

FZJ-2022-04909

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structure and Dynamics of Human Chemokine CCL16—Implications for Biological Activity

Weiergräber, O. H. (Corresponding author)FZJ* ; Petrović, D. ; Kislat, A. ; Pattky, M. ; Fabig, J. ; Batra-Safferling, R.FZJ* ; Schulte am Esch, J. ; Hänel, K.FZJ* ; Huhn, C. ; Strodel, B.FZJ* ; Homey, B. ; Willbold, D. (Corresponding author)FZJ*

2022
MDPI Basel

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Please use a persistent id in citations: http://hdl.handle.net/2128/32936  doi:10.3390/biom12111588

Abstract: 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.

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Contributing Institute(s):

1. Strukturbiochemie (IBI-7)

Research Program(s):

1. 5241 - Molecular Information Processing in Cellular Systems (POF4-524) (POF4-524)
2. SFB 974 A11 - Kommunikation und Systemrelevanz bei Leberschädigung und Regeneration (190586431) (190586431)

Appears in the scientific report 2022

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