Journal article
Novel FXXFF and FXXMF motifs in androgen receptor cofactors mediate high affinity and specific interactions with the ligand-binding domain.
- Abstract:
-
Upon hormone binding, a hydrophobic coactivator binding groove is induced in the androgen receptor (AR) ligand-binding domain (LBD). This groove serves as high affinity docking site for alpha-helical FXXLF motifs present in the AR N-terminal domain and in AR cofactors. Study of the amino acid requirements at position +4 of the AR FXXLF motif revealed that most amino acid substitutions strongly reduced or completely abrogated AR LBD interaction. Strong interactions were still observed followin...
Expand abstract
- Publication status:
- Published
Actions
Access Document
- Publisher copy:
- 10.1074/jbc.m602567200
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:
- Journal of biological chemistry
- Volume:
- 281
- Issue:
- 28
- Pages:
- 19407-19416
- Publication date:
- 2006-07-01
- DOI:
- EISSN:
-
1083-351X
- ISSN:
-
0021-9258
- Source identifiers:
-
284893
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:284893
- UUID:
-
uuid:1c5a99db-708d-4d70-a40e-ccc70c14f4db
- Local pid:
- pubs:284893
- Deposit date:
- 2012-12-19
Terms of use
- Copyright date:
- 2006
If you are the owner of this record, you can report an update to it here: Report update to this record