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| {{STRUCTURE_1kd7| PDB=1kd7 | SCENE= }} | | {{STRUCTURE_1kd7| PDB=1kd7 | SCENE= }} |
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| '''Crystal structure of an extracellular domain fragment of human BAFF'''
| | ===Crystal structure of an extracellular domain fragment of human BAFF=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11827482}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11827482 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11827482}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Beta-sheet shandwich]] | | [[Category: Beta-sheet shandwich]] |
| [[Category: Tnf]] | | [[Category: Tnf]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:35:52 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:09:41 2008'' |
