5h7n
From Proteopedia
Crystal structure of human NLRP12-PYD with a MBP tag
Structural highlights
DiseaseNAL12_HUMAN NLRP12-associated hereditary periodic fever syndrome. The disease is caused by mutations affecting the gene represented in this entry. FunctionMALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.NAL12_HUMAN May mediate activation of CASP1 via ASC and promote activation of NF-kappa-B via IKK. Publication Abstract from PubMedCrystallization 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. Design of an expression system to enhance MBP-mediated crystallization.,Jin T, Chuenchor W, Jiang J, Cheng J, Li Y, Fang K, Huang M, Smith P, Xiao TS Sci Rep. 2017 Jan 23;7:40991. doi: 10.1038/srep40991. PMID:28112203[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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