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本文引用的文献

1
Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.血色素沉着症蛋白HFE的晶体结构及其与转铁蛋白受体相互作用的表征
Cell. 1998 Apr 3;93(1):111-23. doi: 10.1016/s0092-8674(00)81151-4.
2
The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding.血色素沉着症基因产物与转铁蛋白受体形成复合物，并降低其与配体结合的亲和力。
Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1472-7. doi: 10.1073/pnas.95.4.1472.
3
Exon/intron structure of the human transferrin receptor gene.人类转铁蛋白受体基因的外显子/内含子结构。
Gene. 1997 Oct 15;199(1-2):123-31. doi: 10.1016/s0378-1119(97)00356-9.
4
The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells.正常细胞和肿瘤细胞中铁的代谢与转运的分子机制。
Biochim Biophys Acta. 1997 Mar 14;1331(1):1-40. doi: 10.1016/s0304-4157(96)00014-7.
5
RGD and other recognition sequences for integrins.RGD及其他整联蛋白识别序列。
Annu Rev Cell Dev Biol. 1996;12:697-715. doi: 10.1146/annurev.cellbio.12.1.697.
6
Functional analysis of human/chicken transferrin receptor chimeras indicates that the carboxy-terminal region is important for ligand binding.人/鸡转铁蛋白受体嵌合体的功能分析表明，羧基末端区域对配体结合很重要。
Eur J Biochem. 1996 Jan 15;235(1-2):9-17. doi: 10.1111/j.1432-1033.1996.0009u.x.
7
2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region.2.0人纤连蛋白包含RGD环和协同区域的四结构域片段的晶体结构。
Cell. 1996 Jan 12;84(1):155-64. doi: 10.1016/s0092-8674(00)81002-8.
8
A region of the C-terminal portion of the human transferrin receptor contains an asparagine-linked glycosylation site critical for receptor structure and function.人转铁蛋白受体C末端区域含有一个对受体结构和功能至关重要的天冬酰胺连接的糖基化位点。
J Biol Chem. 1993 Jun 15;268(17):12780-6.
9
The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet GP IIb-IIIa receptor.血小板糖蛋白IIb-IIIa受体拮抗剂弗拉沃立定的核磁共振溶液结构
J Mol Biol. 1993 Aug 5;232(3):907-25. doi: 10.1006/jmbi.1993.1439.
10
Signal-dependent membrane protein trafficking in the endocytic pathway.内吞途径中信号依赖的膜蛋白运输
Annu Rev Cell Biol. 1993;9:129-61. doi: 10.1146/annurev.cb.09.110193.001021.

转铁蛋白受体中一个保守的RGD（精氨酸-甘氨酸-天冬氨酸）基序是与转铁蛋白结合所必需的。

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

作者信息

Dubljevic V, Sali A, Goding J W

机构信息

Department of Pathology and Immunology, Monash Medical School, Alfred Hospital, Prahran, Victoria 3181, Australia.

出版信息

Biochem J. 1999 Jul 1;341 ( Pt 1)(Pt 1):11-4.

PMID:10377239
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1220324/
Abstract

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.

摘要

转铁蛋白受体在其C末端区域含有一个高度保守的精氨酸-甘氨酸-天冬氨酸（RGD）序列，据认为转铁蛋白就是在此处结合。RGD序列通常参与细胞黏附。该序列对于转铁蛋白结合至关重要，这表明介导铁摄取的分子与细胞黏附分子之间可能存在进化联系。