A conserved RGD (Arg-Gly-Asp) motif in the transferrin receptor is required for binding to transferrin

被引：52

作者：

Dubljevic, V ^{[1
]}

Sali, A ^{[1
]}

Goding, JW ^{[1
]}

机构：

[1] Monash Univ, Alfred Hosp, Sch Med, Dept Pathol & Immunol, Prahran, Vic 3181, Australia

来源：

BIOCHEMICAL JOURNAL | 1999年 / 341卷

关键词：

affinity binding; conformational epitopes; iron uptake; secreted phosphatase fusion protein;

D O I：

10.1042/0264-6021:3410011

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：

The transferrin receptor contains a highly conserved Arg-Gly-Asp (RGD) sequence in the C-terminal region where transferrin is thought to bind. RGD sequences are commonly involved in cell adhesion. This sequence is crucial for transferrin binding, suggesting possible evolutionary links between molecules mediating iron uptake and cell adhesion.

引用

页码：11 / 14

页数：4

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