1xu1: Difference between revisions
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|PDB= 1xu1 |SIZE=350|CAPTION= <scene name='initialview01'>1xu1</scene>, resolution 1.90Å | |PDB= 1xu1 |SIZE=350|CAPTION= <scene name='initialview01'>1xu1</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NI:NICKEL (II) ION'>NI</scene> | |LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Tnfsf13, APRIL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), TNFRSF13B, TACI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= Tnfsf13, APRIL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), TNFRSF13B, TACI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1u5x|1u5x]], [[1u5y|1u5y]], [[1u5z|1u5z]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xu1 OCA], [http://www.ebi.ac.uk/pdbsum/1xu1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xu1 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==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. | 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== | ==About this Structure== | ||
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[[Category: Yan, M.]] | [[Category: Yan, M.]] | ||
[[Category: Yin, J.]] | [[Category: Yin, J.]] | ||
[[Category: crd]] | [[Category: crd]] | ||
[[Category: cysteine-rich]] | [[Category: cysteine-rich]] | ||
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[[Category: tnfsf]] | [[Category: tnfsf]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:54:36 2008'' | ||
Revision as of 00:54, 31 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | |||||||
| Gene: | Tnfsf13, APRIL (Mus musculus), TNFRSF13B, TACI (Homo sapiens) | ||||||
| Related: | 1u5x, 1u5y, 1u5z
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of APRIL bound to TACI
OverviewOverview
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 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
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