1xu1: Difference between revisions

Revision as of 08:49, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1xu1.png

Template:STRUCTURE 1xu1

The crystal structure of APRIL bound to TACIThe crystal structure of APRIL bound to TACI

Template:ABSTRACT PUBMED 15542592

About this StructureAbout this Structure

1XU1 is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 08:49:20 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1xu1.gif|left|200px]]
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 {{STRUCTURE_1xu1|  PDB=1xu1  |  SCENE=  }}
-'''The crystal structure of APRIL bound to TACI'''
+===The crystal structure of APRIL bound to TACI===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15542592}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15542592 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15542592}}
 ==About this Structure==
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 [[Category: Receptor]]
 [[Category: Tnfsf]]
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