@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}
}

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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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