In this section
@article{Jalan:2020:10.1038/s41589-019-0435-y,
author = {Jalan, A and Sammon, D and Hartgerink, J and Brear, P and Stott, K and Hamaia, S and Hunter, E and Walker, D and Leitinger, B and Farndale, R},
doi = {10.1038/s41589-019-0435-y},
journal = {Nature Chemical Biology},
pages = {423--429},
title = {Chain alignment of collagen I deciphered using computationally designed heterotrimers},
url = {http://dx.doi.org/10.1038/s41589-019-0435-y},
volume = {16},
year = {2020}
}
TY - JOUR
AB - The most abundant member of the collagen protein family, collagen I (COL1), is composed of two similar (chain A) and one unique (chain B) polypeptides that self-assemble with one amino acid offset into a heterotrimeric triple helix. Given the offset, chain B can occupy either the leading (BAA), middle (ABA) or trailing (AAB) position of the triple helix, yielding three isomeric biomacromolecules with different protein recognition properties. Despite five decades of intensive research, there is no consensus on the position of chain B in COL1. Here, three triple-helical heterotrimers that each contained a putative Von Willebrand Factor (VWF) and discoidin domain receptor (DDR) recognition sequence from COL1 were designed with chain B permutated in all three positions. AAB demonstrated a strong preference for both VWF and DDR and also induced higher levels of cellular DDR phosphorylation. Thus, we resolve this long-standing mystery and show that COL1 adopts an AAB register.
AU - Jalan,A
AU - Sammon,D
AU - Hartgerink,J
AU - Brear,P
AU - Stott,K
AU - Hamaia,S
AU - Hunter,E
AU - Walker,D
AU - Leitinger,B
AU - Farndale,R
DO - 10.1038/s41589-019-0435-y
EP - 429
PY - 2020///
SN - 1552-4450
SP - 423
TI - Chain alignment of collagen I deciphered using computationally designed heterotrimers
T2 - Nature Chemical Biology
UR - http://dx.doi.org/10.1038/s41589-019-0435-y
UR - https://www.nature.com/articles/s41589-019-0435-y
UR - http://hdl.handle.net/10044/1/75308
VL - 16
ER -
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