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1kd7
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(New page: 200px<br /> <applet load="1kd7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kd7, resolution 2.80Å" /> '''Crystal structure o...)
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Revision as of 15:43, 12 November 2007
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Crystal structure of an extracellular domain fragment of human BAFF
Overview
B cell activating factor (BAFF), a ligand belonging to the tumor necrosis, factor (TNF) family, plays a critical role in regulating survival and, activation of peripheral B cell populations and has been associated with, autoimmune disease. BAFF is known to interact with three receptors, BCMA, TACI and BAFF-R, that have distant similarities with other receptors of, the TNF family. We have determined the crystal structure of the, TNF-homologous domain of BAFF at 2.8 A resolution. The structure reveals, significant differences when compared to other TNF family members, including an unusually long D-E loop that participates in the formation of, a deep, concave and negatively charged region in the putative receptor, binding site. The BAFF structure was further used to generate a homology, model of APRIL, a closely related TNF family ligand that also binds to, BCMA and TACI, but not BAFF-R. Analysis of the putative receptor binding, sites of BAFF and APRIL suggests that differences in the D-E loop, structure and electrostatic surface potentials may be important for, determining binding specificities for BCMA, TACI and BAFF-R.
About this Structure
1KD7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of extracellular human BAFF, a TNF family member that stimulates B lymphocytes., Karpusas M, Cachero TG, Qian F, Boriack-Sjodin A, Mullen C, Strauch K, Hsu YM, Kalled SL, J Mol Biol. 2002 Feb 1;315(5):1145-54. PMID:11827482
Page seeded by OCA on Mon Nov 12 17:50:04 2007
