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. 2024 Jan 7;22(1):37. doi: 10.3390/md22010037

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© 2024 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Model of molecular interactions between Hf-(D)Tensilin and collagen fibrils in dermis of sea-cucumber Holothuria forskali. Crosslinking of collagen fibrils (co) depends on two types of interaction: (1) dimerization or oligomerization of tensilin molecules via positively and negatively charged amino acid interactions (pni) and non-covalent cation-π interactions (cpi) at the C-terminal part of tensilin (red circles), and (2) binding of the NTR-TIMP-like domain (ntd) at the N-terminal part of tensilin with sulfates (s) on glycosaminoglycan (GAG) sidechains of proteoglycans (pg) attached via their protein core (pc) to the surface of collagen fibrils (green circles). (Redrawn and modified from reference [45]).