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PDBsum entry 1kd7
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Membrane protein
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PDB id
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1kd7
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of extracellular human baff, A tnf family member that stimulates b lymphocytes.
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Authors
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M.Karpusas,
T.G.Cachero,
F.Qian,
A.Boriack-Sjodin,
C.Mullen,
K.Strauch,
Y.M.Hsu,
S.L.Kalled.
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Ref.
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J Mol Biol, 2002,
315,
1145-1154.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Figure 1. Representative region of the final 2F[o] - F[c]
electron density map contoured at 1.0 s.
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Figure 2.
Figure 2. Crystal structure of human BAFF. (a) BAFF trimer
in ribbon representation. Monomers are colored differently and
b-strands and N and C-terminal residues are labeled for the
green-colored monomer. Also shown in the ball-and-stick
representation are the disulfide bridge in red and the
glycosylation site Asn242 in turquoise. (b) Space-filling model
of BAFF viewed along the 3-fold axis from the top of the trimer.
The arrows point to the putative receptor binding sites. The
Figure was made with RIBBONS.[47]
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2002,
315,
1145-1154)
copyright 2002.
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