1KD7

Crystal structure of an extracellular domain fragment of human BAFF

Summary for 1KD7

• Entry DOI: 10.2210/pdb1kd7/pdb
• Descriptor: TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 13B (1 entity in total)
• Functional Keywords: beta-sheet shandwich, tnf, membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Single-pass type II membrane protein. Tumor necrosis factor ligand superfamily member 13b, soluble form: Secreted: Q9Y275
• Total number of polymer chains: 6
• Total formula weight: 111348.49

Authors

Karpusas, M.,Cachero, T.G.,Qian, F.,Boriack-Sjodin, A.,Mullen, C.,Strauch, K.,Hsu, Y.-M.,Kalled, S.L. (deposition date: 2001-11-12, release date: 2002-11-12, Last modification date: 2024-11-06)

Primary citation

Karpusas, M.,Cachero, T.G.,Qian, F.,Boriack-Sjodin, A.,Mullen, C.,Strauch, K.,Hsu, Y.-M.,Kalled, S.L.
Crystal Structure of Extracellular Human BAFF, a TNF Family Member that Stimulates B Lymphocytes
J.Mol.Biol., 315:1145-1154, 2002

PubMed Abstract: 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.

PubMed: 11827482
DOI: 10.1006/jmbi.2001.5296

Experimental method

X-RAY DIFFRACTION (2.8 Å)