C-type lectin

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Lectin C-type domain
PDB 1jzn EBI.jpg
Pentameric structure of rattlesnake venom lectin which is a galactose binding lectin. [1] [2]
Identifiers
SymbolLectin_C
Pfam PF00059
InterPro IPR001304
SMART CLECT
PROSITE PS50041
SCOP2 2msb / SCOPe / SUPFAM
CDD cd00037
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

A C-type lectin (CLEC) is a type of carbohydrate-binding protein known as a lectin. [3] The C-type designation is from their requirement for calcium for binding. [4] Proteins that contain C-type lectin domains have a diverse range of functions including cell-cell adhesion, immune response to pathogens and apoptosis. [5] [6]

Contents

Classification

Drickamer et al. classified C-type lectins into 7 subgroups (I to VII) based on the order of the various protein domains in each protein. [7] This classification was subsequently updated in 2002, leading to seven additional groups (VIII to XIV). [8] Most recently, three further subgroups were added (XV to XVII). [3]

GroupNameAssociated domains
I Lecticans EGF, Sushi, Ig and Link domains
II Asialoglycoprotein and DC receptorsNone
III Collectins None
IV Selectins Sushi and EGF domains
V NK - cell receptorsNone
VIMulti-CTLD endocytic receptorsFnII and Ricin domains
VIIReg groupNone
VIII Chondrolectin, Layilin None
IX Tetranectin None
X Polycystin WSC, REJ, PKD domains
XIAttractin (ATRN)PSI, EGF and CUB domains
XII Eosinophil major basic protein (EMBP)None
XIII DGCR2 None
XIV Thrombomodulin, CD93, CD248, CLEC14A EGF domains [9]
XV Bimlec None
XVISEEC SCP and EGF domains
XVIICBCP/Frem1/QBRICKCSPG repeats and CalX-beta domains

CLECs include:

The "NK Cell lectin-like receptors" are a very closely related group: [10]

Additional proteins containing this domain include:

Related Research Articles

Pattern recognition receptors (PRRs) play a crucial role in the proper function of the innate immune system. PRRs are germline-encoded host sensors, which detect molecules typical for the pathogens. They are proteins expressed mainly by cells of the innate immune system, such as dendritic cells, macrophages, monocytes, neutrophils, as well as by epithelial cells, to identify two classes of molecules: pathogen-associated molecular patterns (PAMPs), which are associated with microbial pathogens, and damage-associated molecular patterns (DAMPs), which are associated with components of host's cells that are released during cell damage or death. They are also called primitive pattern recognition receptors because they evolved before other parts of the immune system, particularly before adaptive immunity. PRRs also mediate the initiation of antigen-specific adaptive immune response and release of inflammatory cytokines.

Scavenger receptors are a large and diverse superfamily of cell surface receptors. Its properties were first recorded in 1970 by Drs. Brown and Goldstein, with the defining property being the ability to bind and remove modified low density lipoproteins (LDL). Today scavenger receptors are known to be involved in a wide range of processes, such as: homeostasis, apoptosis, inflammatory diseases and pathogen clearance. Scavenger receptors are mainly found on myeloid cells and other cells that bind to numerous ligands, primarily endogenous and modified host-molecules together with pathogen-associated molecular patterns(PAMPs), and remove them. The Kupffer cells in the liver are particularly rich in scavenger receptors, includes SR-A I, SR-A II, and MARCO.

Collectins (collagen-containing C-type lectins) are a part of the innate immune system. They form a family of collagenous Ca2+-dependent defense lectins, which are found in animals. Collectins are soluble pattern recognition receptors (PRRs). Their function is to bind to oligosaccharide structure or lipids that are on the surface of microorganisms. Like other PRRs they bind pathogen-associated molecular patterns (PAMPs) and danger-associated molecular patterns (DAMPs) of oligosaccharide origin. Binding of collectins to microorganisms may trigger elimination of microorganisms by aggregation, complement activation, opsonization, activation of phagocytosis, or inhibition of microbial growth. Other functions of collectins are modulation of inflammatory, allergic responses, adaptive immune system and clearance of apoptotic cells.

<span class="mw-page-title-main">CD2</span> Cell adhesion molecule found on the surface of T cells and natural killer

CD2 is a cell adhesion molecule found on the surface of T cells and natural killer (NK) cells. It has also been called T-cell surface antigen T11/Leu-5, LFA-2, LFA-3 receptor, erythrocyte receptor and rosette receptor.

Siglecs(Sialic acid-binding immunoglobulin-type lectins) are cell surface proteins that bind sialic acid. They are found primarily on the surface of immune cells and are a subset of the I-type lectins. There are 14 different mammalian Siglecs, providing an array of different functions based on cell surface receptor-ligand interactions.

<span class="mw-page-title-main">KLRD1</span>

CD94, also known as killer cell lectin-like receptor subfamily D, member 1 (KLRD1) is a human gene.

<span class="mw-page-title-main">CLEC4M</span> Protein-coding gene in the species Homo sapiens

C-type lectin domain family 4 member M is a protein that in humans is encoded by the CLEC4M gene. CLEC4M has also been designated as CD299.

<span class="mw-page-title-main">CLEC7A</span> Protein-coding gene in humans

C-type lectin domain family 7 member A or Dectin-1 is a protein that in humans is encoded by the CLEC7A gene. CLEC7A is a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. The encoded glycoprotein is a small type II membrane receptor with an extracellular C-type lectin-like domain fold and a cytoplasmic domain with a partial immunoreceptor tyrosine-based activation motif. It functions as a pattern-recognition receptor for a variety of β-1,3-linked and β-1,6-linked glucans from fungi and plants, and in this way plays a role in innate immune response. Expression is found on myeloid dendritic cells, monocytes, macrophages and B cells. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. This gene is closely linked to other CTL/CTLD superfamily members on chromosome 12p13 in the natural killer gene complex region.

<span class="mw-page-title-main">KLRC4</span> Protein-coding gene in the species Homo sapiens

NKG2-F type II integral membrane protein is a protein that in humans is encoded by the KLRC4 gene.

<span class="mw-page-title-main">SIGLEC7</span> Protein-coding gene in the species Homo sapiens

Sialic acid-binding Ig-like lectin 7 is a protein that in humans is encoded by the SIGLEC7 gene. SIGLEC7 has also been designated as CD328.

<span class="mw-page-title-main">KLRC2</span> Protein-coding gene in humans

NKG2-C type II integral membrane protein or NKG2C is a protein that in humans is encoded by the KLRC2 gene. It is also known as or cluster of differentiation 159c (CD159c).

<span class="mw-page-title-main">CLEC1B</span> Protein-coding gene in humans

C-type lectin domain family 1 member B is a protein that in humans is encoded by the CLEC1B gene.

<span class="mw-page-title-main">CD248</span> Protein-coding gene in the species Homo sapiens

Endosialin is a protein that in humans is encoded by the CD248 gene.

<span class="mw-page-title-main">CLEC4A</span> Protein-coding gene in humans

C-type lectin domain family 4 member A is a protein that in humans is encoded by the CLEC4A gene.

<span class="mw-page-title-main">CLEC1A</span> Protein-coding gene in humans

C-type lectin domain family 1 member A is a protein that in humans is encoded by the CLEC1A gene.

<span class="mw-page-title-main">CLEC2B</span> Protein-coding gene in humans

C-type lectin domain family 2 member B is a protein that in humans is encoded by the CLEC2B gene.

<span class="mw-page-title-main">CLEC12A</span> Protein-coding gene in humans

C-type lectin domain family 12 member A is a protein that in humans is encoded by the CLEC12A gene.

<span class="mw-page-title-main">NOD-like receptor</span> Class of proteins

The nucleotide-binding oligomerization domain-like receptors, or NOD-like receptors (NLRs), are intracellular sensors of pathogen-associated molecular patterns (PAMPs) that enter the cell via phagocytosis or pores, and damage-associated molecular patterns (DAMPs) that are associated with cell stress. They are types of pattern recognition receptors (PRRs), and play key roles in the regulation of innate immune response. NLRs can cooperate with toll-like receptors (TLRs) and regulate inflammatory and apoptotic response.

Glycan arrays, like that offered by the Consortium for Functional Glycomics (CFG), National Center for Functional Glycomics (NCFG) and Z Biotech, LLC, contain carbohydrate compounds that can be screened with lectins, antibodies or cell receptors to define carbohydrate specificity and identify ligands. Glycan array screening works in much the same way as other microarray that is used for instance to study gene expression DNA microarrays or protein interaction Protein microarrays.

<span class="mw-page-title-main">Collectin-12</span> Protein found in humans

Collectin-12, also known as collectin subfamily member 12, is a collectin protein that in humans is encoded by the COLEC12 gene.

References

  1. Walker JR, Nagar B, Young NM, Hirama T, Rini JM (April 2004). "X-ray crystal structure of a galactose-specific C-type lectin possessing a novel decameric quaternary structure". Biochemistry. 43 (13): 3783–92. doi:10.1021/bi035871a. PMID   15049685.
  2. Mahla RS, Reddy MC, Prasad DV, Kumar H (September 2013). "Sweeten PAMPs: Role of Sugar Complexed PAMPs in Innate Immunity and Vaccine Biology". Frontiers in Immunology. 4: 248. doi: 10.3389/fimmu.2013.00248 . PMC   3759294 . PMID   24032031.
  3. 1 2 Zelensky AN, Gready JE (December 2005). "The C-type lectin-like domain superfamily". FEBS J. 272 (24): 6179–217. doi:10.1111/j.1742-4658.2005.05031.x. PMID   16336259. S2CID   7084402.
  4. C-Type+Lectin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  5. Drickamer K (October 1999). "C-type lectin-like domains". Curr. Opin. Struct. Biol. 9 (5): 585–90. doi:10.1016/S0959-440X(99)00009-3. PMID   10508765.
  6. Cambi A, Figdor C (May 2009). "Necrosis: C-type lectins sense cell death". Curr. Biol. 19 (9): R375–8. Bibcode:2009CBio...19.R375C. doi: 10.1016/j.cub.2009.03.032 . PMID   19439262. S2CID   17409821.
  7. Drickamer K (1993). "Evolution of Ca(2+)-dependent animal lectins". Prog. Nucleic Acid Res. Mol. Biol. Progress in Nucleic Acid Research and Molecular Biology. 45: 207–32. doi: 10.1016/S0079-6603(08)60870-3 . ISBN   978-0-12-540045-9. PMID   8341801.
  8. Drickamer K, Fadden AJ (2002). "Genomic analysis of C-type lectins". Biochem. Soc. Symp. 69 (69): 59–72. doi:10.1042/bss0690059. PMID   12655774.
  9. Khan, K. A.; McMurray, J. L.; Mohammed, F.; Bicknell, R. (2019). "C-type lectin domain group 14 proteins in vascular biology, cancer and inflammation". FEBS Journal. 286 (17): 3299–3332. doi:10.1111/febs.14985. PMC   6852297 . PMID   31287944.
  10. NK+Cell+Lectin-Like+Receptors at the U.S. National Library of Medicine Medical Subject Headings (MeSH)