4v46: Difference between revisions

Latest revision as of 08:02, 29 March 2023

Crystal structure of the BAFF-BAFF-R complex

Structural highlights

4v46 is a 120 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entries 1otz and 1p0t. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	MG
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TN13B_HUMAN Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA. TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-cells and the B-cell response.^[1] Isoform 2 seems to inhibit isoform 1 secretion and bioactivity (By similarity).^[2]

Publication Abstract from PubMed

B-cell activating factor (BAFF) is a key regulator of B-lymphocyte development. Its biological role is mediated by the specific receptors BCMA, TACI and BAFF-R. We have determined the crystal structure of the extracellular domain of BAFF-R bound to BAFF at a resolution of 3.3 A. The cysteine-rich domain (CRD) of the BAFF-R extracellular domain adopts a beta-hairpin structure and binds to the virus-like BAFF cage in a 1:1 molar ratio. The conserved DxL motif of BAFF-R is located on the tip of the beta-turn and is indispensable in the binding of BAFF. The crystal structure shows that a unique dimeric contact occurs between the BAFF-R monomers in the virus-like cage complex. The extracellular domain of TACI contains two CRDs, both of which contain the DxL motif. Modeling of TACI-BAFF complex suggests that both CDRs simultaneously interact with the BAFF dimer in the virus-like cage.

Crystal structure of the BAFF-BAFF-R complex and its implications for receptor activation.,Kim HM, Yu KS, Lee ME, Shin DR, Kim YS, Paik SG, Yoo OJ, Lee H, Lee JO Nat Struct Biol. 2003 May;10(5):342-8. PMID:12715002^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yu G, Boone T, Delaney J, Hawkins N, Kelley M, Ramakrishnan M, McCabe S, Qiu WR, Kornuc M, Xia XZ, Guo J, Stolina M, Boyle WJ, Sarosi I, Hsu H, Senaldi G, Theill LE. APRIL and TALL-I and receptors BCMA and TACI: system for regulating humoral immunity. Nat Immunol. 2000 Sep;1(3):252-6. PMID:10973284 doi:10.1038/79802
↑ Yu G, Boone T, Delaney J, Hawkins N, Kelley M, Ramakrishnan M, McCabe S, Qiu WR, Kornuc M, Xia XZ, Guo J, Stolina M, Boyle WJ, Sarosi I, Hsu H, Senaldi G, Theill LE. APRIL and TALL-I and receptors BCMA and TACI: system for regulating humoral immunity. Nat Immunol. 2000 Sep;1(3):252-6. PMID:10973284 doi:10.1038/79802
↑ Kim HM, Yu KS, Lee ME, Shin DR, Kim YS, Paik SG, Yoo OJ, Lee H, Lee JO. Crystal structure of the BAFF-BAFF-R complex and its implications for receptor activation. Nat Struct Biol. 2003 May;10(5):342-8. PMID:12715002 doi:10.1038/nsb925

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Yu G, Boone T, Delaney J, Hawkins N, Kelley M, Ramakrishnan M, McCabe S, Qiu WR, Kornuc M, Xia XZ, Guo J, Stolina M, Boyle WJ, Sarosi I, Hsu H, Senaldi G, Theill LE. APRIL and TALL-I and receptors BCMA and TACI: system for regulating humoral immunity. Nat Immunol. 2000 Sep;1(3):252-6. PMID:10973284 doi:10.1038/79802

[2] Yu G, Boone T, Delaney J, Hawkins N, Kelley M, Ramakrishnan M, McCabe S, Qiu WR, Kornuc M, Xia XZ, Guo J, Stolina M, Boyle WJ, Sarosi I, Hsu H, Senaldi G, Theill LE. APRIL and TALL-I and receptors BCMA and TACI: system for regulating humoral immunity. Nat Immunol. 2000 Sep;1(3):252-6. PMID:10973284 doi:10.1038/79802

[3] Kim HM, Yu KS, Lee ME, Shin DR, Kim YS, Paik SG, Yoo OJ, Lee H, Lee JO. Crystal structure of the BAFF-BAFF-R complex and its implications for receptor activation. Nat Struct Biol. 2003 May;10(5):342-8. PMID:12715002 doi:10.1038/nsb925

[1]

[2]

[3]

@@ Line 3: / Line 3: @@
 <StructureSection load='4v46' size='340' side='right'caption='[[4v46]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4v46]] is a 120 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1otz 1otz] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1p0t 1p0t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V46 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V46 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4v46]] is a 120 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1otz 1otz] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1p0t 1p0t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V46 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4v46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v46 OCA], [http://pdbe.org/4v46 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v46 RCSB], [http://www.ebi.ac.uk/pdbsum/4v46 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v46 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4v46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v46 OCA], [https://pdbe.org/4v46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v46 RCSB], [https://www.ebi.ac.uk/pdbsum/4v46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v46 ProSAT]</span></td></tr>
 </table>
-== Disease ==
-[[http://www.uniprot.org/uniprot/TR13C_HUMAN TR13C_HUMAN]] Defects in TNFRSF13C are the cause of immunodeficiency common variable type 4 (CVID4) [MIM:[http://omim.org/entry/613494 613494]]; also called antibody deficiency due to BAFFR defect. CVID4 is a primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low.<ref>PMID:19666484</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/TN13B_HUMAN TN13B_HUMAN]] Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA. TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-cells and the B-cell response.<ref>PMID:10973284</ref>   Isoform 2 seems to inhibit isoform 1 secretion and bioactivity (By similarity).<ref>PMID:10973284</ref>  [[http://www.uniprot.org/uniprot/TR13C_HUMAN TR13C_HUMAN]] B-cell receptor specific for TNFSF13B/TALL1/BAFF/BLyS. Promotes the survival of mature B-cells and the B-cell response.<ref>PMID:11591325</ref> <ref>PMID:12387744</ref>
+[https://www.uniprot.org/uniprot/TN13B_HUMAN TN13B_HUMAN] Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA. TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-cells and the B-cell response.<ref>PMID:10973284</ref>   Isoform 2 seems to inhibit isoform 1 secretion and bioactivity (By similarity).<ref>PMID:10973284</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 20: @@
 ==See Also==
-*[[Tumor necrosis factor receptor|Tumor necrosis factor receptor]]
+*[[Tumor necrosis factor receptor 3D structures|Tumor necrosis factor receptor 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Kim, H M]]
+[[Category: Kim HM]]
-[[Category: Kim, Y S]]
+[[Category: Kim YS]]
-[[Category: Lee, H]]
+[[Category: Lee H]]
-[[Category: Lee, J O]]
+[[Category: Lee J-O]]
-[[Category: Lee, M E]]
+[[Category: Lee ME]]
-[[Category: Paik, S G]]
+[[Category: Paik SG]]
-[[Category: Shin, D R]]
+[[Category: Shin DR]]
-[[Category: Yoo, O J]]
+[[Category: Yoo OJ]]
-[[Category: Yu, K S]]
+[[Category: Yu KS]]
-[[Category: Cytokine]]

4v46: Difference between revisions

Latest revision as of 08:02, 29 March 2023

Crystal structure of the BAFF-BAFF-R complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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