Imperial College London

ProfessorKurtDrickamer

Faculty of Natural SciencesDepartment of Life Sciences

Chair in Biochemistry
 
 
 
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Contact

 

+44 (0)20 7594 5282k.drickamer

 
 
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Location

 

606Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Taylor:2015:10.1016/j.sbi.2015.06.003,
author = {Taylor, ME and Drickamer, K},
doi = {10.1016/j.sbi.2015.06.003},
journal = {Current Opinion in Structural Biology},
pages = {26--34},
title = {Recent insights into structures and functions of C-type lectins in the immune system},
url = {http://dx.doi.org/10.1016/j.sbi.2015.06.003},
volume = {34},
year = {2015}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - The majority of the C-type lectin-like domains in the human genome likely to bind sugars have been investigated structurally, although novel mechanisms of sugar binding are still being discovered. In the immune system, adhesion and endocytic receptors that bind endogenous mammalian glycans are often conserved, while pathogen-binding C-type lectins on cells of the innate immune system are more divergent. Lack of orthology between some human and mouse receptors, as well as overlapping specificities of many receptors and formation of receptor hetero-oligomers, can make it difficult to define the roles of individual receptors. There is good evidence that C-type lectins initiate signalling pathways in several different ways, but this function remains the least well understood from a mechanistic perspective.
AU - Taylor,ME
AU - Drickamer,K
DO - 10.1016/j.sbi.2015.06.003
EP - 34
PY - 2015///
SN - 0959-440X
SP - 26
TI - Recent insights into structures and functions of C-type lectins in the immune system
T2 - Current Opinion in Structural Biology
UR - http://dx.doi.org/10.1016/j.sbi.2015.06.003
UR - http://hdl.handle.net/10044/1/25024
VL - 34
ER -