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Identification of residues in CD6 which are critical for ligand binding.

Abstract：

:CD6 is a member of the scavenger receptor cysteine rich protein superfamily (SRCRSF). This family includes many cell surface proteins whose three-dimensional structures and functions are presently not well understood. The extracellular region of CD6 includes 3 SRCR domains. The membrane proximal SRCR domain specifically binds the activated leukocyte cell adhesion molecule (ALCAM), a CD6 ligand belonging to the immunoglobulin superfamily. CD6-ALCAM interactions mediate immune cell adhesion and are implicated in T cell maturation and the regulation of T cell function. On the basis of SRCRSF sequence comparison, a mutagenesis analysis of the membrane proximal SRCR domain of CD6 (CD6D3) has been carried out. Fifteen mutants were characterized. Three CD6 residues were identified in a region of low sequence conservation which, when mutated, abolish ligand binding but not the binding to a panel of conformationally sensitive anti-CD6 mAbs. This study provides the first analysis of residues critical for ligand binding to a member of the SRCRSF.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Bodian DL,Skonier JE,Bowen MA,Neubauer M,Siadak AW,Aruffo A,Bajorath J

doi

10.1021/bi962560+

subject

Has Abstract

pub_date

1997-03-04 00:00:00

pages

2637-41

issue

9

eissn

0006-2960

issn

1520-4995

pii

bi962560+

journal_volume

36

pub_type

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