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Structures of SALSA/DMBT1 SRCR domains reveal the conserved ligand-binding mechanism of the ancient SRCR-fold

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,...

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Publication status:
Published
Peer review status:
Peer reviewed

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Institution:
Univesrity of Oxford
Division:
MSD
Department:
Pathology Dunn School
Subgroup:
Pathology Dunn School
Role:
Author
ORCID:
0000-0001-5345-5103
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Subgroup:
Pathology Dunn School
Role:
Author
ORCID:
0000-0001-9287-8053
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Subgroup:
Pathology Dunn School
Role:
Author
ORCID:
0000-0002-7877-3543
More from this funder
Grant:
100298/Z/12/A
100298/Z/12/Z
209194/Z/17/Z
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:

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