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Functional evolution of IGF2:IGF2R domain 11 binding generates novel structural interactions and a specific IGF2 antagonist.

Abstract:

Among the 15 extracellular domains of the mannose 6-phosphate/insulin-like growth factor-2 receptor (M6P/IGF2R), domain 11 has evolved a binding site for IGF2 to negatively regulate ligand bioavailability and mammalian growth. Despite the highly evolved structural loops of the IGF2:domain 11 binding site, affinity-enhancing AB loop mutations suggest that binding is modifiable. Here we examine the extent to which IGF2:domain 11 affinity, and its specificity over IGF1, can be enhanced, and we e...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1073/pnas.1513023113

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Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author
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Engineering and Physical Sciences Research Council More from this funder
Cancer Research UK More from this funder
National Institute for Health Research More from this funder
Algerian Government More from this funder
Agilent Technologies More from this funder
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Publisher:
National Academy of Sciences Publisher's website
Journal:
Proceedings of the National Academy of Sciences Journal website
Publication date:
2016-05-02
Acceptance date:
2016-03-31
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
Source identifiers:
619315
Language:
English
Keywords:
Pubs id:
pubs:619315
UUID:
uuid:c9183f7d-440b-4efe-8ac6-9dbca4dcf295
Local pid:
pubs:619315
Deposit date:
2016-10-05

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