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INSIGHT INTO E-SELECTIN(SLASH)LIGAND INTERACTION FROM THE CRYSTAL STRUCTURE AND MUTAGENESIS OF THE LEC(SLASH)EGF DOMAINSINSIGHT INTO E-SELECTIN(SLASH)LIGAND INTERACTION FROM THE CRYSTAL STRUCTURE AND MUTAGENESIS OF THE LEC(SLASH)EGF DOMAINS
Structural highlights
FunctionLYAM2_HUMAN Cell-surface glycoprotein having a role in immunoadhesion. Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with PSGL1/SELPLG. May have a role in capillary morphogenesis.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe three-dimensional structure of the ligand-binding region of human E-selectin has been determined at 2.0 A resolution. 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. These features of the E-selectin/ligand interaction have important implications for understanding the recruitment of leukocytes to sites of inflammation. Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains.,Graves BJ, Crowther RL, Chandran C, Rumberger JM, Li S, Huang KS, Presky DH, Familletti PC, Wolitzky BA, Burns DK Nature. 1994 Feb 10;367(6463):532-8. PMID:7509040[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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