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Structures of the EphA2 receptor at the membrane: Role of lipid interactions

Abstract:

Ephs are transmembrane receptors that mediate cell-cell signaling. The N-terminal ectodomain binds ligands and enables receptor clustering, which activates the intracellular kinase. Relatively little is known about the function of the membrane-proximal fibronectin domain 2 (FN2) of the ectodomain. Multiscale molecular dynamics simulations reveal that FN2 interacts with lipid bilayers via a site comprising K441, R443, R465, Q462, S464,...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1016/j.str.2015.11.008

Authors


More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author
ORCID:
0000-0003-4524-4773
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author
ORCID:
0000-0001-6112-5198
More by this author
Institution:
University of Oxford
Division:
Structural Biology
Department:
Nuffield Department of Clinical Medicine
Oxford college:
Jesus College
Role:
Author
ORCID:
0000-0002-3834-1893
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Oxford college:
Corpus Christi College
Role:
Author
ORCID:
0000-0001-6360-7959

Contributors

Role:
C375/A10976
Publisher:
Cell Press Publisher's website
Journal:
Structure Journal website
Volume:
24
Pages:
337-347
Publication date:
2017-12-24
Acceptance date:
2015-11-13
DOI:
EISSN:
1878-4186
ISSN:
1878-4186
Source identifiers:
573489
Keywords:
Pubs id:
pubs:573489
UUID:
uuid:bc441f33-c039-42e9-a7fc-4e62d539c0b6
Local pid:
pubs:573489
Deposit date:
2015-11-16

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