Identification of Residues in CD6 Which Are Critical for Ligand Binding

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• 作者：Dale L. Bodian ; John E. Skonier ; Michael A. Bowen ; Michael Neubauer ; Anthony W. Siadak ; Alejandro Aruffo ; and Jü ; rgen Bajorath
• 刊名：Biochemistry
• 出版年：1997
• 出版时间：March 4, 1997
• 年：1997
• 卷：36
• 期：9
• 页码：2637 - 2641
• 全文大小：352K
• 年卷期：v.36,no.9(March 4, 1997)
• ISSN：1520-4995

文摘

CD6 is a member of the scavenger receptor cysteine rich proteinsuperfamily (SRCRSF).This family includes many cell surface proteins whosethree-dimensional structures and functions arepresently not well understood. The extracellular region of CD6includes 3 SRCR domains. The membraneproximal SRCR domain specifically binds the activated leukocyte celladhesion molecule (ALCAM), aCD6 ligand belonging to the immunoglobulin superfamily.CD6-ALCAM interactions mediate immunecell adhesion and are implicated in T cell maturation and theregulation of T cell function. On the basisof SRCRSF sequence comparison, a mutagenesis analysis of the membraneproximal SRCR domain ofCD6 (CD6D3) has been carried out. Fifteen mutants werecharacterized. Three CD6 residues wereidentified in a region of low sequence conservation which, whenmutated, abolish ligand binding but notthe binding to a panel of conformationally sensitive anti-CD6 mAbs.This study provides the first analysisof residues critical for ligand binding to a member of theSRCRSF.