preprints.org > biology and life sciences > biochemistry and molecular biology > doi: 10.20944/preprints202308.1015.v1

Preprint Review Version 1 Preserved in Portico This version is not peer-reviewed

Version 1 : Received: 14 August 2023 / Approved: 14 August 2023 / Online: 14 August 2023 (10:51:46 CEST)

: Extra- and intra-cellular activity occurs under the direction of numerous inter-molecular interactions, and in any tissue or cell, molecules are densely packed, thus promoting those molecular interactions. Galectins and chemokines, the focus of this review, are small, protein effector molecules that mediate various cellular functions, in particular cell adhesion and migration, as well as cell signaling/activation. In the past, researchers have reported that combinations of these (and other) effector molecules act separately, yet sometimes in concert, but nevertheless physically apart and via their individual cell receptors. This view that each effector molecule functions independently of the other limits our thinking about functional versatility and cooperation, and, in turn, ignores the prospect of physiologically important inter-molecular interactions, especially when both molecules are present or co-expressed in the same cellular environment. This review is focused on such protein-protein interactions with chemokines and galectins, their homo- and hetero-oligomeric structures that they can form, and the functional consequences of those paired interactions.

galectin; chemokine; structure; function; NMR; modeling

Biology and Life Sciences, Biochemistry and Molecular Biology

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