HYDROPHOBIC CLUSTER-ANALYSIS REVEALS DUPLICATION IN THE EXTERNAL STRUCTURE OF HUMAN ALPHA-INTERFERON RECEPTOR AND HOMOLOGY WITH GAMMA-INTERFERON RECEPTOR EXTERNAL DOMAIN

被引：19

作者：

GABORIAUD, C

UZE, G

LUTFALLA, G

MOGENSEN, K

机构：

[1] CNRS, UPR 274,IRSC,ONCOL VIRALE LAB,7 RUE GUY MOQUET, BP 8, F-94801 VILLEJUIF, FRANCE

[2] UNIV PARIS 06, MINERAL CRISTALLOG LAB, CNRS, UNITE 09, F-75252 PARIS 05, FRANCE

[3] UNIV PARIS 07, MINERAL CRISTALLOG LAB, CNRS, UNITE 09, F-75252 PARIS 05, FRANCE

来源：

FEBS LETTERS | 1990年 / 269卷 / 01期

关键词：

Amino acid sequence comparison; Interferon receptor; Protein homology;

D O I：

10.1016/0014-5793(90)81103-U

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：

Evidence is presented, based on sequence comparison according to Hydrophobic Cluster Analysis, of a structural and evolutionary relationship between the human α/β-interferon receptor and the human and mouse γ-interferon receptor. These results predict that the human α/β-interferon receptor extracellular part is organised in two homologous subdomains connected by a proline linker. They also predict that both subdomains present some homologies to the external domain of mouse and human γ interferon receptor. © 1990.

引用

页码：1 / 3

页数：3

共 11 条

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