LPAM-1
macromolecular complex found in Homo sapiens
Integrin α4β7 (Lymphocyte Peyer’s patch adhesion molecule-1) is an integrin heterodimer composed of CD49d (alpha-4) subunit and beta-7 subunit noncovalently linked. LPAM-1 is expressed on the cell surface of leukocytes. This receptor is involved in lymphocyte trafficking pathway to site of inflammation in intestinal tissues.
Structure
LPAM-1 α and β subunits are composed of a large extracellular domain, a short transmembrane region and a cytoplasmic tail. Its ligand specificity depends on both α4 and β7 subunits.
The binding head of the β7 chain has three metal-binding sites that contributes to the cation-dependent (Ca2+, Mg2+ and Mn2+) allosteric conformational activation of the integrin α4β7. These three sites are ligand-induced metal-binding site (LIMBS), metal ion-dependent adhesion site (MIDAS) and adjacent to metal ion-dependent adhesion site (ADMIDAS). LIMBS and ADMIDAS sites regulates the cell adherence of lymphocyte by affecting the adhesion or de-adhesion of the integrin to its ligand.
In the α4 subunit, Tyr187 was identified as a critical amino acid in integrin α4β7-mediated cell adhesion. Its mutation affects interactions between integrin α4β7 and its ligands.
This brief starts where responsible research should: with the source description of “LPAM-1” as macromolecular complex found in Homo sapiens. Everything that follows is an evidence route, not borrowed authority.
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The citation trail is more important than the brevity of the summary: it shows where individual claims can be examined in context. The source revision retrieved here is dated Aug 19, 2026. The linked authority identifier is Q107516023. None of the 0 selected statements returned an explicit reference.
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This entry incorporates text from “LPAM-1” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.