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cysteinyl leukotriene receptor 1 (CysLTR1, cysteinyl leukotriene D4 receptor, LTD4 receptor, HG55, HMTMF81)

Function: - receptor for cysteinyl leukotrienes mediating bronchoconstriction of individuals with & without asthma - stimulation by LTD4 results in contraction & proliferation of smooth muscle, edema, eosinophil migration & damage to the mucus layer in the lung - this response is mediated via a G-protein that activates a phosphatidylinositol-Ca+2 second messenger system - the rank order of affinities for the leukotrienes is LTD4 >> LTE4 = LTC4 >> LTB4 Structure: belongs to the G-protein coupled receptor 1 family Compartment: cell membrane Expression: - widely expressed, with highest levels in spleen & peripheral blood leukocytes - lower expression in several tissues, such as lung (mostly in smooth muscle bundles & alveolar macrophages), placenta, small intestine, pancreas, colon & heart Pharmacology: - selective antagonists, such as montelukast (singulair), zafirlukast (accolate) & pranlukast (Onon), are used in the treatment of the asthma

Related

leukotriene C

General

glycoprotein leukotriene receptor G-protein coupled receptor; serpentine receptor

Properties

SIZE: MW = 39 kD entity length = 337 aa COMPARTMENT: cellular membrane MOTIF: exoplasmic domain {1-28} MOTIF: N-glycosylation site {N6} transmembrane domain {29-49} cytoplasmic loop {50-57} transmembrane domain {58-78} exoplasmic loop {79-106} MOTIF: cysteine residue {C96} MODIFICATION: cysteine residue {C173} transmembrane domain {107-127} cytoplasmic loop {128-141} transmembrane domain {142-162} exoplasmic loop {163-193} MOTIF: N-glycosylation site {N169} cysteine residue {C173} MODIFICATION: cysteine residue {C96} N-glycosylation site {N180} transmembrane domain {194-214} cytoplasmic loop {215-230} transmembrane domain {231-251} exoplasmic loop {252-276} MOTIF: N-glycosylation site {N262} transmembrane domain {277-297} cytoplasmic domain {298-337}

Database Correlations

OMIM 300201 UniProt Q9Y271 Pfam PF00001 Kegg hsa:1080

References

UniProt :accession Q9Y271