selectin
Sign in to saveAlso known as selectins, Selectin, C-type lectin-like domain, protein family, IPR033991
The selectins (cluster of differentiation 62 or CD62) are a family of cell adhesion molecules (or CAMs). All selectins are single-chain transmembrane glycoproteins that share similar properties to C-type lectins due to a related amino terminus and calcium-dependent binding. Selectins bind to sugar moieties and so are considered to be a type of lectin, cell adhesion proteins that bind sugar polymers.
Key facts
- Protein family.Symbol
- Selectin
- Protein family.Name
- Selectin
- Protein family.image
- Pselectin.PNG
- Protein family.width
- 200px
- Protein family.caption
- Crystallographic structure of P-selectin lectin bound to sugar, shown in sticks.
- Protein family.InterPro
- IPR002396
- Protein family.Membranome superfamily
- 12
via Wikipedia infobox
Research
26,679 papers- Selectin-Mediated Signaling-Shedding Light on the Regulation of Integrin Activity in Neutrophils.Cells · 2022
- P-selectin glycoprotein ligand-1 in T cells.Current opinion in hematology · 2017
- P- and E- selectin in venous thrombosis and non-venous pathologies.Journal of thrombosis and haemostasis : JTH · 2022
- Selectin-carbohydrate interactions during inflammation and metastasis.Glycoconjugate journal · 1997
- Selectin antagonists : therapeutic potential in asthma and COPD.Treatments in respiratory medicine · 2005
via PubMed
~11 min read
Article
11 sectionsContents
- Structure
- Types
- Etymology
- Function
- Bonding mechanisms
- Role in cancer
- Organ selectivity
- Research
- See also
- References
- External links
The selectins (cluster of differentiation 62 or CD62) are a family of cell adhesion molecules (or CAMs). All selectins are single-chain transmembrane glycoproteins that share similar properties to C-type lectins due to a related amino terminus and calcium-dependent binding. Selectins bind to sugar moieties and so are considered to be a type of lectin, cell adhesion proteins that bind sugar polymers.
== Structure == All three known members of the selectin family (L-, E-, and P-selectin) share a similar cassette structure: an N-terminal, calcium-dependent lectin domain, an epidermal growth factor (EGF)-like domain, a variable number of consensus repeat units (2, 6, and 9 for L-, E-, and P-selectin, respectively), a transmembrane domain (TM) and an intracellular cytoplasmic tail (cyto). The transmembrane and cytoplasmic parts are not conserved across the selectins being responsible for their targeting to different compartments. Though they share common elements, their tissue distribution and binding kinetics are quite different, reflecting their divergent roles in various pathophysiological processes.