The structure of the CARD8 caspase-recruitment domain suggests its association with the FIIND domain and procaspases through adjacent surfaces

Jin, Tengchuan; Huang, M.; Smith, Patrick; Jiang, Jiansheng; Xiao, Tsan Sam

doi:10.1107/s1744309113010075

Cited by 15 publications

(20 citation statements)

References 31 publications

(36 reference statements)

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“…In the 22 fusion proteins with the linker sequence NAAAEF, the EF sequence corresponds to an Eco RI site (GAA TTC) that was used for cloning (H. E. Xu, Personal Communication), although this was is not mentioned in the accompanying publications . Similarly, in the three fusion proteins with the linker sequence NAVD, the VD dipeptide probably corresponds to a Sal I restriction site (GTC GAC), but this could not be verified from the published information …”

Section: Origin and Diversity Of Inter‐domain Linkersmentioning

confidence: 99%

“…28,32,35,37,40 Similarly, in the three fusion proteins with the linker sequence NAVD, the VD dipeptide probably corresponds to a SalI restriction site (GTC GAC), but this could not be verified from the published information. [49][50][51] Of course it would be useful to know if there is a particular linker or linkers that are most likely to yield useful crystals. Unfortunately, however, a definitive answer to this question is lacking because negative results are rarely reported.…”

Section: Mbp As a Crystallization Chaperonementioning

confidence: 99%

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Crystal structures of MBP fusion proteins

Waugh

2016

Protein Science

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Although chaperone-assisted protein crystallization remains a comparatively rare undertaking, the number of crystal structures of polypeptides fused to maltose-binding protein (MBP) that have been deposited in the Protein Data Bank (PDB) has grown dramatically during the past decade. Altogether, 102 fusion protein structures were detected by Basic Local Alignment Search Tool (BLAST) analysis. Collectively, these structures comprise a range of sizes, space groups, and resolutions that are typical of the PDB as a whole. While most of these MBP fusion proteins were equipped with short inter-domain linkers to increase their rigidity, fusion proteins with long linkers have also been crystallized. In some cases, surface entropy reduction mutations in MBP appear to have facilitated the formation of crystals. A comparison of the structures of fused and unfused proteins, where both are available, reveals that MBP-mediated structural distortions are very rare.

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Section: Origin and Diversity Of Inter‐domain Linkersmentioning

confidence: 99%

Section: Mbp As a Crystallization Chaperonementioning

confidence: 99%

Crystal structures of MBP fusion proteins

Waugh

2016

Protein Science

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“…The short linker of VD residues followed by the first helical residues of the target proteins may help enhance crystallization. Even though this strategy has resulted in success for some of our targets such as the NLRP1 CARD47, and CARD8 CARD48, and the AIM2 PYD domain47 (Fig. 2b,c), it has failed for other targets such as the zebrafish IGBP1-CARD and human NLRP1-PYD (sequences are listed in Table S2).…”

Section: Resultsmentioning

confidence: 99%

“…Expression and purification of the MBP-tagged proteins have been described previously4748. Briefly, transformed BL21 (DE3) Codon Plus RIPL cells (Stratagene, Santa Clara, CA) were grown at 37 °C and protein expression was induced at 18 °C for at least two hours with 0.3 mM IPTG.…”

Section: Methodsmentioning

confidence: 99%

“…Inspired by the successful examples of using MBP as a crystallization chaperone, we designed an expression vector (V28E) coding an E. coli MBP protein1346 followed by a very short linker with amino acid sequence of valine and aspartate encoded by the Sal I restriction enzyme site (GTCGAC). This vector has limited success in expression and crystallization of several fusion proteins for PYD and CARD domains474849. Here we sought to systematically explore the usage of linkers of various lengths and test their effects on crystallization of death domain superfamily members.…”

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confidence: 99%

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Design of an expression system to enhance MBP-mediated crystallization

Jin

Chuenchor

Jiang

et al. 2017

Sci Rep

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Crystallization chaperones have been used to facilitate the crystallization of challenging proteins. Even though the maltose-binding protein (MBP) is one of the most commonly used crystallization chaperones, the design of optimal expression constructs for crystallization of MBP fusion proteins remains a challenge. To increase the success rate of MBP-facilitated crystallization, a series of expression vectors have been designed with either a short flexible linker or a set of rigid helical linkers. Seven death domain superfamily members were tested for crystallization with this set of vectors, six of which had never been crystallized before. All of the seven targets were crystallized, and their structures were determined using at least one of the vectors. Our successful crystallization of all of the targets demonstrates the validity of our approach and expands the arsenal of the crystallization chaperone toolkit, which may be applicable to crystallization of other difficult protein targets, as well as to other crystallization chaperones.

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The versatile roles of CARDs in regulating apoptosis, inflammation, and NF-κB signaling

Kao

Yang

et al. 2014

Apoptosis

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CARD subfamily is the second largest subfamily in the DD superfamily that plays important roles in regulating various signaling pathways, including but not limited to NF-kB activation signaling, apoptosis signaling and inflammatory signaling. The CARD subfamily contains 33 human CARD-containing proteins, regulating the assembly of many signaling complexes, including apoptosome, inflammsome, nodosome, the CBM complex, PIDDosome, the TRAF2 complex, and the MAVS signalosome, by homotypic CARD-CARD interactions. The mechanism of how CARDs find the right binding partner to form a specific complex remains unclear. This review uses different classification schemes to update the classification of CARD-containing proteins. Combining the classification based on domain structures, functions, associated signaling complexes, and roles would help better understand the structural and function diversity of CARD-containing proteins. This review also summarizes recent structural studies on CARDs. Especially, the CARD-containing complexes can be divided into the homodimeric, heterodimeric, oligomeric, filamentous CARD complexes and the CARD-ubiquitin complex. This review will give an overview of the versatile roles of CARDs in regulating signaling transduction, as well as the therapeutic drugs targeting CARD-containing proteins.

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The structure of the CARD8 caspase-recruitment domain suggests its association with the FIIND domain and procaspases through adjacent surfaces

Cited by 15 publications

References 31 publications

Crystal structures of MBP fusion proteins

Crystal structures of MBP fusion proteins

Design of an expression system to enhance MBP-mediated crystallization

The versatile roles of CARDs in regulating apoptosis, inflammation, and NF-κB signaling

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