View source for 1osx

[[Image:1osx.gif|left|200px]]<br />
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'''Solution Structure of the Extracellular Domain of BLyS Receptor 3 (BR3)'''<br />

==Overview==
BAFF/BLyS, a member of the tumor necrosis family (TNF) superfamily of, ligands, is a crucial survival factor for B cells. BAFF binds three, receptors, TACI, BCMA, and BR3, with signaling through BR3 being essential, for promoting B cell function. Typical TNF receptor (TNFR) family members, bind their cognate ligands through interactions with two cysteine-rich, domains (CRDs). However, the extracellular domain (ECD) of BR3 consists of, only a partial CRD, with cysteine spacing distinct from other modules, described previously. Herein, we report the solution structure of the BR3, ECD. A core region of only 19 residues adopts a stable structure in, solution. The BR3 fold is analogous to the first half of a canonical TNFR, CRD but is stabilized by an additional noncanonical disulfide bond., BAFF-binding determinants were identified by shotgun alanine-scanning, mutagenesis of the BR3 ECD expressed on phage. Several of the key, BAFF-binding residues are presented from a beta-turn that we have shown, previously to be sufficient for ligand binding when transferred to a, structured beta-hairpin scaffold [Kayagaki, N., Yan, M., Seshasayee, D., Wang, H., Lee, W., French, D. M., Grewal, I. S., Cochran, A. G., Gordon, N. C., Yin, J., Starovasnik, M. A, and Dixit, V. M. (2002) Immunity 10, 515-524]. Outside of the turn, mutagenesis identifies additional, hydrophobic contacts that enhance the BAFF-BR3 interaction. The crystal, structure of the minimal hairpin peptide, bhpBR3, in complex with BAFF, reveals intimate packing of the six-residue BR3 turn into a cavity on the, ligand surface. Thus, BR3 binds BAFF through a highly focused interaction, site, unprecedented in the TNFR family.

==About this Structure==
1OSX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OSX OCA]. 

==Reference==
BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site., Gordon NC, Pan B, Hymowitz SG, Yin J, Kelley RF, Cochran AG, Yan M, Dixit VM, Fairbrother WJ, Starovasnik MA, Biochemistry. 2003 May 27;42(20):5977-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12755599 12755599]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Cochran, A.G.]]
[[Category: Dixit, V.M.]]
[[Category: Fairbrother, W.J.]]
[[Category: Gordon, N.C.]]
[[Category: Hymowitz, S.G.]]
[[Category: Kelley, R.F.]]
[[Category: Pan, B.]]
[[Category: Starovasnik, M.A.]]
[[Category: Yan, M.]]
[[Category: Yin, J.P.]]
[[Category: cysteine-rich domain]]
[[Category: extracellular domain]]
[[Category: tumor necrosis factor receptor]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:36:17 2007''