5h7n

Crystal structure of human NLRP12-PYD with a MBP tag

spinqualitylabelsall models 5h7n, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5h7n is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.849Å Ligands: EDO, GLC, PEG, PRD_900010, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease NAL12_HUMAN NLRP12-associated hereditary periodic fever syndrome. The disease is caused by mutations affecting the gene represented in this entry. Function MALE_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 PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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