View source for 4v46


==Crystal structure of the BAFF-BAFF-R complex==
<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 [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" 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'>[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>
== Function ==
[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 ==
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<ref>PMID:12715002</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4v46" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tumor necrosis factor receptor 3D structures|Tumor necrosis factor receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Kim HM]]
[[Category: Kim YS]]
[[Category: Lee H]]
[[Category: Lee J-O]]
[[Category: Lee ME]]
[[Category: Paik SG]]
[[Category: Shin DR]]
[[Category: Yoo OJ]]
[[Category: Yu KS]]