共 22 条
The adhesive binding site of cadherins revisited
被引:32
作者:

Shan, WS
论文数: 0 引用数: 0
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机构: CUNY Mt Sinai Sch Med, Dept Physiol & Biophys, Struct Biol Program, New York, NY 10029 USA

Koch, A
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机构: CUNY Mt Sinai Sch Med, Dept Physiol & Biophys, Struct Biol Program, New York, NY 10029 USA

Murray, J
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机构: CUNY Mt Sinai Sch Med, Dept Physiol & Biophys, Struct Biol Program, New York, NY 10029 USA

Colman, DR
论文数: 0 引用数: 0
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机构: CUNY Mt Sinai Sch Med, Dept Physiol & Biophys, Struct Biol Program, New York, NY 10029 USA

Shapiro, L
论文数: 0 引用数: 0
h-index: 0
机构: CUNY Mt Sinai Sch Med, Dept Physiol & Biophys, Struct Biol Program, New York, NY 10029 USA
机构:
[1] CUNY Mt Sinai Sch Med, Dept Physiol & Biophys, Struct Biol Program, New York, NY 10029 USA
[2] CUNY Mt Sinai Sch Med, Brookdale Ctr Biochem & Mol Biol, New York, NY 10029 USA
关键词:
cadherin;
cell adhesion;
homophilic binding;
D O I:
10.1016/S0301-4622(99)00115-5
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Cadherins are single-pass transmembrane proteins that, through their homophilic specificity, function in selective cell adhesion and sorting. They have a modular structure that includes an ectodomain composed of tandem 'cadherin domains,' which have a beta-sandwich topology similar to that of immunoglobulin domains. Some early experiments suggest that, for the 'classical' cadherins, the adhesive specificity is encoded in the membrane-distal amino-terminal cadherin domain. Here, we review these data, and present new data that supports this idea. (C) 1999 Elsevier Science B.V. All rights reserved.
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页码:157 / 163
页数:7
相关论文
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