原创力文档the cysteine-rich interdomain region from the highly variable plasmodium falciparum erythrocyte membrane protein-1 exhibits a conserved structure从高度可变的cysteine-rich interdomain地区恶性疟原虫红细胞膜蛋白1展览守恒的结构.pdfVIP
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the cysteine-rich interdomain region from the highly variable plasmodium falciparum erythrocyte membrane protein-1 exhibits a conserved structure从高度可变的cysteine-rich interdomain地区恶性疟原虫红细胞膜蛋白1展览守恒的结构
The Cysteine-Rich Interdomain Region from the Highly
Variable Plasmodium falciparum Erythrocyte Membrane
Protein-1 Exhibits a Conserved Structure
1. 1. 1¤a 2 1¤b
Michael M. Klein , Apostolos G. Gittis , Hua-Poo Su , Morris O. Makobongo , Jaime M. Moore ,
2¤c 2 1
Sanjay Singh , Louis H. Miller , David N. Garboczi *
1 Structural Biology Section, Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, Maryland, United
States of America, 2 Malaria Vaccine Development Branch, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, Maryland, United
States of America
Abstract
Plasmodium falciparum malaria parasites, living in red blood cells, express proteins of the erythrocyte membrane protein-1
(PfEMP1) family on the red blood cell surface. The binding of PfEMP1 molecules to human cell surface receptors mediates
the adherence of infected red blood cells to human tissues. The sequences of the 60 PfEMP1 genes in each parasite genome
vary greatly from parasite to parasite, yet the variant PfEMP1 proteins maintain receptor binding. Almost all parasites
isolated directly from patients bind the human CD36 receptor. Of the several kinds of highly polymorphic cysteine-rich
interdomain region (CIDR) domains classified by sequence, only the CIDR1a domains bind CD36. Here we describe the
CD36-binding portion of a CIDR1a domain, MC179, as a bundle of three a-helices that are connected by a loop and three
additional
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