Journal article
Structure of signal-regulatory protein alpha: a link to antigen receptor evolution.
- Abstract:
-
Signal-regulatory protein alpha (SIRPalpha) is a myeloid membrane receptor that interacts with the membrane protein CD47, a marker of self. We have solved the structure of the complete extracellular portion of SIRPalpha, comprising three immunoglobulin superfamily domains, by x-ray crystallography to 2.5 A resolution. These data, together with previous data on the N-terminal domain and its ligand CD47 (possessing a single immunoglobulin superfamily domain), show that the CD47-SIRPalpha intera...
Expand abstract
- Publication status:
- Published
Actions
Access Document
- Publisher copy:
- 10.1074/jbc.m109.017566
Why is the content I wish to access not available via ORA?
Bibliographic data (the information relating to research outputs) and full-text items (e.g. articles, theses, reports, etc.) arrive in ORA from several different sources. Unfortunately we are not able to make available the full-text for every research output.
Please contact the ORA team (
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
Content may be unavailable for the following four reasons
-
Version unsuitable
-
We have not obtained a suitable full-text for a given research output. See this page for more information.
-
Recently completed
-
Sometimes content is held in ORA but is unavailable for a fixed period of time to comply with the policies and wishes of rights holders.
-
Permissions
-
All content made available in ORA should comply with relevant rights, such as copyright. See this page for more information.
-
Clearance
-
Some thesis volumes scanned as part of the digitisation scheme funded by Dr Leonard Polonsky are currently unavailable due to sensitive material or uncleared third-party copyright content. We are attempting to contact authors whose theses are affected.
Alternative access to the full-text
You may be able to access the full-text directly from the publisher's website using the 'Publisher Copy' link in the 'Links & Downloads' box from a research output's ORA record page. This method may require an institutional or individual subscription to the journal/resource.
Authors
Bibliographic Details
- Journal:
- The Journal of biological chemistry
- Volume:
- 284
- Issue:
- 39
- Pages:
- 26613-26619
- Publication date:
- 2009-09-05
- DOI:
- EISSN:
-
1083-351X
- ISSN:
-
0021-9258
- URN:
-
uuid:1a8a57ec-3ed1-461f-8d84-b6f4a0cbac84
- Source identifiers:
-
9251
- Local pid:
- pubs:9251
Item Description
- Language:
- English
- Keywords:
Terms of use
- Copyright date:
- 2009
If you are the owner of this record, you can report an update to it here: Report update to this record