Imperial College London
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ProfessorErhardHohenester

Faculty of Natural Sciences, Department of Life Sciences

Professor of Structural Matrix Biology
 
 
 
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Contact

 

e.hohenester

 
 
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Location

 

404ASir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Briggs:2018:10.1016/j.str.2018.03.014,
author = {Briggs, DC and Hohenester, E},
doi = {10.1016/j.str.2018.03.014},
journal = {Structure (London, England : 1993)},
pages = {801--809.e3},
title = {Structural Basis for the Initiation of Glycosaminoglycan Biosynthesis by Human Xylosyltransferase 1.},
url = {http://dx.doi.org/10.1016/j.str.2018.03.014},
volume = {26},
year = {2018}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Proteoglycans (PGs) are essential components of the animal extracellular matrix and are required for cell adhesion, migration, signaling, and immune function. PGs are composed of a core protein and long glycosaminoglycan (GAG) chains, which often specify PG function. GAG biosynthesis is initiated by peptide O-xylosyltransferases, which transfer xylose onto selected serine residues in the core proteins. We have determined crystal structures of human xylosyltransferase 1 (XT1) in complex with the sugar donor, UDP-xylose, and various acceptor peptides. The structures reveal unique active-site features that, in conjunction with functional experiments, explain the substrate specificity of XT1. A constriction within the peptide binding cleft requires the acceptor serine to be followed by glycine or alanine. The remainder of the cleft can accommodate a wide variety of sequences, but with a general preference for acidic residues. These findings provide a framework for understanding the selectivity of GAG attachment.
AU  - Briggs,DC
AU  - Hohenester,E
DO  - 10.1016/j.str.2018.03.014
EP  - 809
PY  - 2018///
SN  - 0969-2126
SP  - 801
TI  - Structural Basis for the Initiation of Glycosaminoglycan Biosynthesis by Human Xylosyltransferase 1.
T2  - Structure (London, England : 1993)
UR  - http://dx.doi.org/10.1016/j.str.2018.03.014
UR  - http://hdl.handle.net/10044/1/58443
VL  - 26
ER  -
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