- Abstract:
-
The scavenger receptor cysteine-rich (SRCR) family of proteins comprises more than 20 membrane-associated and secreted molecules. Characterised by the presence of one or more copies of the ∼110 amino-acid SRCR domain, this class of proteins have widespread functions as antimicrobial molecules, scavenger receptors, and signalling receptors. Despite the high level of structural conservation of SRCR domains, no unifying mechanism for ligand interaction has been described. The SRCR protein SALSA,...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Files:
-
- Publisher copy:
- 10.26508/lsa.201900502
-
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- Publisher:
- Life Science Alliance Publisher's website
- Journal:
- Life Science Alliance Journal website
- Volume:
- 3
- Issue:
- 4
- Article number:
- e201900502
- Publication date:
- 2020-02-25
- Acceptance date:
- 2020-02-14
- DOI:
- ISSN:
-
2575-1077
- Pubs id:
-
1088100
- Local pid:
- pubs:1088100
- Language:
- English
- Keywords:
- Copyright holder:
- Reichhardt et al.
- Copyright date:
- 2020
- Rights statement:
- © 2020 Reichhardt et al. This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/ licenses/by/4.0/)
- License:
- CC Attribution (CC BY)
Journal article
Structures of SALSA/DMBT1 SRCR domains reveal the conserved ligand-binding mechanism of the ancient SRCR-fold
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