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Title: Ficolin-1      
dateReleased:
06-17-2016
privacy:
not applicable
aggregation:
instance of dataset
dateCreated:
07-28-2014
refinement:
curated
ID:
doi:10.6072/H0H41PBV
creators:
Chandrasekhar, Anjana
availability:
available
types:
signaling
description:
Ficolin-1 is a member of the lectin family of proteins, which act as pattern recognition receptors in the innate immune system. Its overall structure resembles other lectins such as L- and H-Ficolin and MBL. The ~35kDa polypeptide has an amino (N)-terminal cysteine-rich region, a middle stretch of a collagen-like sequence, and a fibrinogen-like domain in the carboxy (C)-terminus. Three identical polypeptides form a structural (triple helical) subunit, with the help of the collagen-like domain. Further oligomerization of this subunit results in the tetrameric functional form (composed of 12 polypeptides). The polypeptides in the structural subunit are cross-linked by disulphide bonds in the N-terminal region. The fibrinogen-like domain forms a globular structure. Ficolin-1 recognizes specific acetylated sugars on pathogen surfaces. Unlike other ficolins and MBL, which are synthesized by the liver and found in serum, ficolin-1 is mainly synthesized by monocytes and neutrophils, and exhibit surface or granular expression along with presence in serum. Further, ficolin-1 also recognizes sialic acid, a component found in host cell membranes, as a ligand. These characteristics attribute distinct functions to ficolin-1 in regulation of immune response.
accessURL: https://doi.org/10.6072/H0H41PBV
storedIn:
UCSD Molecule Pages
qualifier:
not compressed
format:
HTML
accessType:
landing page
authentication:
none
authorization:
none
abbreviation:
UCSD
homePage: http://www.ucsd.edu/
ID:
SCR:011625
name:
University of California at San Diego
abbreviation:
NSGM
homePage: http://www.signaling-gateway.org/
ID:
SCR:006907
name:
UCSD-Nature Signaling Gateway