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Crystal structure of the BAFF-BAFF-R complex and its implications for receptor activation

机译：BAFF-BAFF-R复合物的晶体结构及其对受体活化的影响

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摘要

B-cell activating factor (BAFF) is a key regulator of B-lymphocyte development. Its biological role is mediated by the specific receptors BCMA, TACT 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 Angstrom. 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 TACT-BAFF complex suggests that both CDRs simultaneously interact with the BAFF dimer in the virus-like cage. [References: 43]
机译：B细胞活化因子（BAFF）是B淋巴细胞发育的关键调节因子。它的生物学作用是由特定的受体BCMA，TACT和BAFF-R介导的。我们已经确定了以3.3埃的分辨率结合到BAFF的BAFF-R的胞外域的晶体结构。 BAFF-R细胞外结构域的富含半胱氨酸的结构域（CRD）采用β-发夹结构，并以1：1的摩尔比结合病毒样BAFF笼。 BAFF-R的保守DxL基序位于β-转角的末端，并且在BAFF的结合中必不可少。晶体结构表明，病毒样笼状复合物中BAFF-R单体之间发生独特的二聚体接触。 TACI的胞外域包含两个CRD，两个都包含DxL基序。 TACT-BAFF复合物的建模表明，两个CDR在病毒样笼中同时与BAFF二聚体相互作用。 [参考：43]

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