Corrigendum: CEACAM1 regulates TIM-3-mediated tolerance and exhaustion.
Corrigendum: CEACAM1 regulates TIM-3-mediated tolerance and exhaustion.
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CRORIGENDUM：CEACAM1调节TIM-3介导的耐受性和精疲力尽。
DOI：
10.1038/nature17421
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发表时间：
2016-08-18
期刊：
影响因子：
64.8
通讯作者：
Blumberg, Richard S.
中科院分区：
文献类型：
--
作者：
Huang, Yu-Hwa;Zhu, Chen;Kondo, Yasuyuki;Anderson, Ana C.;Gandhi, Amit;Russell, Andrew;Dougan, Stephanie K.;Petersen, Britt-Sabina;Melum, Espen;Pertel, Thomas;Clayton, Kiera L.;Raab, Monika;Chen, Qiang;Beauchemin, Nicole;Yazaki, Paul J.;Pyzik, Michal;Ostrowski, Mario A.;Glickman, Jonathan N.;Rudd, Christopher E.;Ploegh, Hidde L.;Franke, Andre;Petsko, Gregory A.;Kuchroo, Vijay K.;Blumberg, Richard S.
In this Letter, we published the crystal structure of a heterodimer of the human (h) CEACAM1 IgV domain and hTIM-3 IgV domain (Protein Data Bank (PDB) accession 4QYC). Since publication, E. Sundberg and S. Almo have questioned our model, and stated that they had obtained better results refining a hCEACAM1–hCEACAM1 homodimer model against our diffracted amplitudes. We confirm that a homodimer model indeed fits our crystallographic data better, as judged by most statistical measures (see Supplementary Table 1). We have therefore withdrawn the deposited heterodimer model (PDB code 4QYC) from the PDB, and replaced it with a more accurate homodimer model (PDB code 5DZL). We thank E. Sundberg and S. Almo for bringing this to our attention, and apologize for any confusion the original structure may have caused.Our error was rooted in an assumption, which now seems to be invalid, that a crystal of a chimaeric two-domain protein should give X-ray diffraction data reflecting both domains. We sought evidence for the hTIM-3 domain in our data using multiple molecular replacement and crystallographic strategies, and also reprocessed the data using lower symmetry space groups in case the hTIM-3 signal was lost in the computational averaging. We now believe that the relatively low resolution of the dataset (3.4 Å) and the similarities between the folds of hCEACAM1 and hTIM-3 make it impossible to model the hTIM-3 IgV domain confidently using the data at hand. To understand how dimeric hCEACAM1 could predominate in a crystal built from a protein construct designed to ensure a 1: 1 ratio of hCEACAM1 and hTIM-3, we performed western blot analyses on the materials used for crystallization, which showed a predominant species of~ 26 kDa, consistent with intact chimaeric protein and minor additional lower molecular mass species, suggesting proteolysis as the reason for the absence of hTIM-3, consistent with the long time (months) required for crystal growth (Supplementary Fig. 1). Considering the strong tendency of CEACAM1 to crystallize as dimers, even a small amount of free homodimer could have preferentially crystallized.
DOI：
10.1073/pnas.1509511112
发表时间：
2015-11-03
影响因子：
11.1
作者：
Bonsor, Daniel A.;Guenther, Sebastian;Sundberg, Eric J.
通讯作者：
Sundberg, Eric J.
影响因子：
64.8
作者：
Huang, Yu-Hwa;Zhu, Chen;Kondo, Yasuyuki;Anderson, Ana C.;Gandhi, Amit;Russell, Andrew;Dougan, Stephanie K.;Petersen, Britt-Sabina;Melum, Espen;Pertel, Thomas;Clayton, Kiera L.;Raab, Monika;Chen, Qiang;Beauchemin, Nicole;Yazaki, Paul J.;Pyzik, Michal;Ostrowski, Mario A.;Glickman, Jonathan N.;Rudd, Christopher E.;Ploegh, Hidde L.;Franke, Andre;Petsko, Gregory A.;Kuchroo, Vijay K.;Blumberg, Richard S.
通讯作者：
Blumberg, Richard S.