1osx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1osx.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1osx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1osx| PDB=1osx | SCENE= }}
{{STRUCTURE_1osx| PDB=1osx | SCENE= }}
-
'''Solution Structure of the Extracellular Domain of BLyS Receptor 3 (BR3)'''
+
===Solution Structure of the Extracellular Domain of BLyS Receptor 3 (BR3)===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12755599}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12755599 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12755599}}
==About this Structure==
==About this Structure==
-
1OSX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSX OCA].
+
1OSX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSX OCA].
==Reference==
==Reference==
Line 35: Line 39:
[[Category: Extracellular domain]]
[[Category: Extracellular domain]]
[[Category: Tumor necrosis factor receptor]]
[[Category: Tumor necrosis factor receptor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:14:36 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:55:30 2008''

Revision as of 13:55, 27 July 2008

Image:1osx.png

Template:STRUCTURE 1osx

Solution Structure of the Extracellular Domain of BLyS Receptor 3 (BR3)

Template:ABSTRACT PUBMED 12755599

About this Structure

1OSX is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from 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:12755599

Page seeded by OCA on Sun Jul 27 16:55:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1osx"
Personal tools