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Article

Crystal structure of the Tspan15 LEL domain reveals a conserved ADAM10 binding site.

Structure (London, England : 1993) - 3 Feb 2022

Lipper Colin H, Gabriel Khal-Hentz, Seegar Tom C M, Dürr Katharina L, Tomlinson Michael G, Blacklow Stephen C

Abstract excerpt

Tetraspanins are four-pass transmembrane proteins that function by regulating trafficking of partner proteins and organizing signaling complexes in the membrane. Tspan15, one of a six-member TspanC8 subfamily, forms a complex that regulates the trafficking, maturation, and substrate selectivity of the transmembrane protease ADAM10, an essential enzyme in mammalian physiology that cleaves a wide variety of...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 34739841
DOI: 10.1016/j.str.2021.10.007
PMCID: PMC8818019

Genes

ADAM10

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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