Journal article
Functional evolution of IGF2:IGF2R domain 11 binding generates novel structural interactions and a specific IGF2 antagonist.
- Abstract:
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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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(Accepted manuscript, pdf, 2.0MB)
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- Publisher copy:
- 10.1073/pnas.1513023113
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Authors
Funding
Engineering and Physical Sciences Research Council
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Cancer Research UK
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National Institute for Health Research
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Algerian Government
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Agilent Technologies
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Bibliographic Details
- 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:
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1091-6490
- ISSN:
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0027-8424
- Source identifiers:
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619315
Item Description
- Language:
- English
- Keywords:
- Pubs id:
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pubs:619315
- UUID:
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uuid:c9183f7d-440b-4efe-8ac6-9dbca4dcf295
- Local pid:
- pubs:619315
- Deposit date:
- 2016-10-05
Terms of use
- Copyright holder:
- National Academy of Sciences
- Copyright date:
- 2016
- Notes:
- © National Academy of Sciences 2016. Publisher's submission form provides automated formatting of AAM. This is the accepted manuscript version of the article. The final version is available online from the National Academy of Sciences at: [10.1073/pnas.1513023113]
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