CHARACTERIZATION OF A HIGHLY STRUCTURED DOMAIN IN TBP2 FROM NEISSERIA-MENINGITIDIS INVOLVED IN BINDING TO HUMAN TRANSFERRIN

被引：40

作者：

VONDERHAAR, RA ^{[1
]}

LEGRAIN, M ^{[1
]}

KOLBE, HVJ ^{[1
]}

JACOBS, E ^{[1
]}

机构：

[1] TRANSGENE SA, F-67082 STRASBOURG, FRANCE

来源：

JOURNAL OF BACTERIOLOGY | 1994年 / 176卷 / 20期

关键词：

D O I：

10.1128/jb.176.20.6207-6213.1994

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The binding of iron-loaded human transferrin at the surface of Neisseria meningitidis is mediated by two polypeptides, Tbp1 and Tbp2. Predicted Tbp amino acid sequences from N. meningitidis strains are highly divergent. This variability is particularly pronounced throughout the Tbp2 polypeptide. In this study, a highly structured and extremely stable Tbp2 domain of about 270 to 290 amino acids which is involved in the binding to transferrin and whose position is well conserved has been characterized. The conservation of such a remarkable structure in a very divergent protein domain (there is only 43% amino acid identity within this region) suggests that is plays an essential biological role and raises a number of questions regarding tbp2 evolution.

引用

页码：6207 / 6213

页数：7

共 25 条

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