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ProteinQ4037752· pop 12· linked from 439 articles

selectin E

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Also known as SELE, endothelial adhesion molecule 1, ELAM-1, CD62 antigen-like family member E, LECAM2, E-selectin, endothelial leukocyte adhesion molecule 1, Leukocyte-endothelial cell adhesion molecule 2

E-selectin, also known as CD62 antigen-like family member E (CD62E), endothelial-leukocyte adhesion molecule 1 (ELAM-1), or leukocyte-endothelial cell adhesion molecule 2 (LECAM2), is a selectin cell adhesion molecule expressed only on endothelial cells activated by cytokines. Like other selectins, it plays an important part in inflammation. In humans, E-selectin is encoded by the SELE gene.

Protein · UniProt

E-selectin

Gene
SELE
Organism
Homo sapiens (Human)
Length
610 aa
Molecular mass
66,655 Da
Evidence
1: Evidence at protein level

Cell-surface glycoprotein having a role in immunoadhesion. Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with SELPLG/PSGL1. May have a role in capillary morphogenesis

3D-structureCalciumCell adhesionCell membraneDisulfide bondEGF-like domainGlycoproteinLectin
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Swiss-Prot (reviewed) · via UniProt

Research

11,636 papers

via PubMed

Clinical Trials

8 registered

via ClinicalTrials.gov

~12 min read

Article

15 sections
Contents
  • Structure
  • Gene and regulation
  • Ligands
  • Function
  • Role in inflammation
  • Role in cancer
  • Pathological relevance
  • Critical illness polyneuromyopathy
  • Pathogen attachment
  • Acute coronary syndrome
  • Nicotine-mediated induction
  • Cerebral aneurysm
  • As a biomarker
  • References
  • External links

E-selectin, also known as CD62 antigen-like family member E (CD62E), endothelial-leukocyte adhesion molecule 1 (ELAM-1), or leukocyte-endothelial cell adhesion molecule 2 (LECAM2), is a selectin cell adhesion molecule expressed only on endothelial cells activated by cytokines. Like other selectins, it plays an important part in inflammation. In humans, E-selectin is encoded by the SELE gene.

==Structure== E selectin has a cassette structure: an N-terminal, C-type lectin domain, an EGF (epidermal-growth-factor)-like domain, 6 Sushi domain (SCR repeat) units, a transmembrane domain (TM) and an intracellular cytoplasmic tail (cyto). The three-dimensional structure of the ligand-binding region of human E-selectin has been determined at 2.0 Å resolution in 1994. The structure reveals limited contact between the two domains and a coordination of Ca2+ not predicted from other C-type lectins. Structure/function analysis indicates a defined region and specific amino-acid side chains that may be involved in ligand binding. The E-selectin bound to sialyl-LewisX (SLeX; NeuNAcα2,3Galβ1,4[Fucα1,3]GlcNAc) tetrasaccharide was solved in 2000.

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