1P0T: Crystal Structure of the Baff-baff-r Complex (Part I)

Citation:
Abstract
B-cell activating factor (BAFF) is a key regulator of B-lymphocyte development. Its biological role is mediated by the specific receptors BCMA, TACI and BAFF-R. We have determined the crystal structure of the extracellular domain of BAFF-R bound to BAFF at a resolution of 3.3 A. The cysteine-rich domain (CRD) of the BAFF-R extracellular domain adopts a beta-hairpin structure and binds to the virus-like BAFF cage in a 1:1 molar ratio. The conserved DxL motif of BAFF-R is located on the tip of the beta-turn and is indispensable in the binding of BAFF. The crystal structure shows that a unique dimeric contact occurs between the BAFF-R monomers in the virus-like cage complex. The extracellular domain of TACI contains two CRDs, both of which contain the DxL motif. Modeling of TACI-BAFF complex suggests that both CDRs simultaneously interact with the BAFF dimer in the virus-like cage.
MMDB ID: 99531
PDB Deposition Date: 2003/3/23
Updated in MMDB: 2012/08 
Experimental Method:
x-ray diffraction
Resolution: 3.3  Å
Source Organism:
Homo sapiens
Similar Structures:
Merged PDB IDs:1OTZ 1P0T
Asymmetric Unit for 1P0T: 120-meric
Molecular Components in 1P0T
Label Count Molecule
Proteins (120 molecules)
60
Tumor Necrosis Factor Ligand Superfamily Member 13B
Molecule annotation
60
Tumor Necrosis Factor Receptor Superfamily Member 13C
Molecule annotation
Chemicals (40 molecules)
1
40
Molecule information is not avaliable.
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