Abstract:
:Malaria during pregnancy is caused when parasite-infected erythrocytes accumulate within the placenta through interactions between the VAR2CSA protein on the infected erythrocyte surface and placental CSPGs (chondroitin sulfate proteoglycans). This interaction is the major target for therapeutics to treat or prevent pregnancy-associated malaria. Here we review the structural characterization of CSPG-binding DBL (Duffy-binding like) domains from VAR2CSA and summarize the growing evidence that the exquisite ligand specificity of VAR2CSA results from the adoption of higher-order architecture in which these domains fold together to form a ligand-binding pocket.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Khunrae P,Higgins MKdoi
10.1042/BST0381337subject
Has Abstractpub_date
2010-10-01 00:00:00pages
1337-41issue
5eissn
0300-5127issn
1470-8752pii
BST0381337journal_volume
38pub_type
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journal_title:Biochemical Society transactions
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journal_title:Biochemical Society transactions
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journal_title:Biochemical Society transactions
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更新日期:2016-02-01 00:00:00
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journal_title:Biochemical Society transactions
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更新日期:2016-02-01 00:00:00
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journal_title:Biochemical Society transactions
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更新日期:2007-11-01 00:00:00
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journal_title:Biochemical Society transactions
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doi:10.1042/bst0311390
更新日期:2003-12-01 00:00:00
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journal_title:Biochemical Society transactions
pub_type: 杂志文章,评审
doi:10.1042/bst0310331
更新日期:2003-04-01 00:00:00
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journal_title:Biochemical Society transactions
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更新日期:2008-06-01 00:00:00
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journal_title:Biochemical Society transactions
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journal_title:Biochemical Society transactions
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journal_title:Biochemical Society transactions
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journal_title:Biochemical Society transactions
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更新日期:2011-01-01 00:00:00
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journal_title:Biochemical Society transactions
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journal_title:Biochemical Society transactions
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journal_title:Biochemical Society transactions
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