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Full length RII of PfEBA-140 binds extensively to erythrocytes (top image), while individual DBL domains show little binding. This indicates that both domains are necessary for erythrocyte binding. |
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== Summary == | == Summary == | ||
Full length RII of PfEBA-140 binds extensively to erythrocytes (top image), while individual DBL domains show little binding. This indicates that both domains are necessary for erythrocyte binding. | Full length RII of PfEBA-140 binds extensively to erythrocytes (top image), while individual DBL domains show little binding. This indicates that both domains are necessary for erythrocyte binding.<ref name="Lin">PMID: 22989878</ref> | ||
== Licensing == | == Licensing == | ||
{{subst:Non-commercial from license selector}} | {{subst:Non-commercial from license selector}} | ||
This research was originally published in The Journal of Biological Chemistry. Daniel H. Lin, Brian M. Malpede, Joseph D. Batchelor and Niraj H. Tolia. Crystal and Solution Structures of Plasmodium falciparum Erythrocyte-binding Antigen 140 Reveal Determinants of Receptor Specificity during Erythrocyte Invasion. J Biol Chem. 2012; Vol:287. 36830-36836. © the American Society for Biochemistry and Molecular Biology." | |||
For other parties using material for noncommercial use: | |||
Other parties are welcome to copy, distribute, transmit and adapt the work — at no cost and without permission — for noncommercial use as long as they attribute the work to the original source using the citation above. | |||
Examples of noncommercial use include: | |||
Reproducing a figure for educational purposes, such as schoolwork or lecture presentations, with attribution. | |||
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==References== | |||
<references /> | |||
