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{Paracuellos:2017:10.1016/j.matbio.2017.02.002,
author = {Paracuellos, P and Kalamajski, S and Bonna, A and Bihan, D and Farndale, RW and Hohenester, E},
doi = {10.1016/j.matbio.2017.02.002},
journal = {Matrix Biology},
pages = {106--116},
title = {Structural and functional analysis of two small leucine-rich repeat proteoglycans, fibromodulin and chondroadherin},
url = {http://dx.doi.org/10.1016/j.matbio.2017.02.002},
volume = {63},
year = {2017}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The small leucine-rich proteoglycans (SLRPs) are important regulators of extracellular matrix assembly and cell signalling. We have determined crystal structures at ~2.2 Å resolution of human fibromodulin and chondroadherin, two collagen-binding SLRPs. Their overall fold is similar to that of the prototypical SLRP, decorin, but unlike decorin neither fibromodulin nor chondroadherin forms a stable dimer. A previously identified binding site for integrin α2β1 maps to an α-helix in the C terminal cap region of chondroadherin. Interrogation of the Collagen Toolkits revealed a unique binding site for chondroadherin in collagen II, and no binding to collagen III. A triple-helical peptide containing the sequence GAOGPSGFQGLOGPOGPO (O is hydroxyproline) forms a stable complex with chondroadherin in solution. In fibrillar collagen I and II, this sequence is aligned with the collagen cross-linking site KGHR, suggesting a role for chondroadherin in cross-linking.
AU  - Paracuellos,P
AU  - Kalamajski,S
AU  - Bonna,A
AU  - Bihan,D
AU  - Farndale,RW
AU  - Hohenester,E
DO  - 10.1016/j.matbio.2017.02.002
EP  - 116
PY  - 2017///
SN  - 1569-1802
SP  - 106
TI  - Structural and functional analysis of two small leucine-rich repeat proteoglycans, fibromodulin and chondroadherin
T2  - Matrix Biology
UR  - http://dx.doi.org/10.1016/j.matbio.2017.02.002
UR  - http://hdl.handle.net/10044/1/44454
VL  - 63
ER  -
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