1xu2

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Revision as of 18:04, 12 November 2007

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spinqualitylabelsall models 1xu2, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

The crystal structure of APRIL bound to BCMA

Overview

TACI is a member of the tumor necrosis factor receptor superfamily and, serves as a key regulator of B cell function. TACI binds two ligands, APRIL and BAFF, with high affinity and contains two cysteine-rich domains, (CRDs) in its extracellular region; in contrast, BCMA and BR3, the other, known high affinity receptors for APRIL and BAFF, respectively, contain, only a single or partial CRD. However, another form of TACI exists wherein, the N-terminal CRD is removed by alternative splicing. We find that this, shorter form is capable of ligand-induced cell signaling and that the, second CRD alone (TACI_d2) contains full affinity for both ligands., Furthermore, we report the solution structure and alanine-scanning, mutagenesis of TACI_d2 along with co-crystal structures of APRIL.TACI_d2, and APRIL.BCMA complexes that together reveal the mechanism by which TACI, engages high affinity ligand binding through a single CRD, and we, highlight sources of ligand-receptor specificity within the APRIL/BAFF, system.

About this Structure

1XU2 is a Protein complex structure of sequences from Homo sapiens and Mus musculus with NI as ligand. Full crystallographic information is available from OCA.

Reference

Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high affinity ligand binding., Hymowitz SG, Patel DR, Wallweber HJ, Runyon S, Yan M, Yin J, Shriver SK, Gordon NC, Pan B, Skelton NJ, Kelley RF, Starovasnik MA, J Biol Chem. 2005 Feb 25;280(8):7218-27. Epub 2004 Nov 12. PMID:15542592

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