Title |
Extended and bent conformations of the mannose receptor family
|
---|---|
Published in |
Cellular and Molecular Life Sciences, January 2008
|
DOI | 10.1007/s00018-007-7497-9 |
Pubmed ID | |
Authors |
O. Llorca |
Abstract |
In mammals, the mannose receptor family consists of four members, Endo180, DEC-205, phospholipase A2 receptor and the mannose receptor. The extracellular domains of all these receptors contain a similar arrangement of domains in which an N-terminal cysteine-rich domain is followed by a single fibronectin type II domain and eight or ten C-type lectin-like domains. This review focuses on the three-dimensional structure of the receptors in the mannose receptor family and its functional implication. Recent research has revealed that several members of this family can exist in at least two configurations: an extended conformation with the N-terminal cysteine-rich domain pointing outwards from the cell membrane and a bent conformation where the N-terminal domains fold back to interact with C-type lectin-like domains at the middle of the structure. Conformational transitions between these two states seem to regulate the interaction of these receptors with ligands and their oligomerization. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
United States | 1 | 2% |
Denmark | 1 | 2% |
France | 1 | 2% |
Unknown | 54 | 95% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 12 | 21% |
Student > Ph. D. Student | 9 | 16% |
Student > Master | 7 | 12% |
Student > Bachelor | 6 | 11% |
Student > Postgraduate | 5 | 9% |
Other | 12 | 21% |
Unknown | 6 | 11% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 23 | 40% |
Medicine and Dentistry | 13 | 23% |
Biochemistry, Genetics and Molecular Biology | 8 | 14% |
Chemistry | 3 | 5% |
Engineering | 2 | 4% |
Other | 3 | 5% |
Unknown | 5 | 9% |