2mab

Untangling the Solution Structure of C-Terminal Domain of Aciniform Spidroin

spinqualitylabelsall models 2mab Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mab is a 2 chain structure with sequence from Trichonephila antipodiana. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function X1WB74_9ARAC Publication Abstract from PubMed C-terminal domains (CTDs) of various spidroins are relatively conserved in the amino acid sequence and have been suggested to perform similar functions. Here, we solved the structure of the CTD of an aciniform spidroin using NMR spectroscopy with a two-point mutant and studied its functional role with several constructs. The CTDs of aciniform, major, and minor ampullate spidroins adopt the same domain-swapping dimeric folding although their sequence identities are 24-40%. Unlike CTDs of major and minor ampullate spidroins, the aciniform CTD had no obvious effects on preventing spidroins from aggregation in storage but slightly enhanced protein assembly under shear force. The differential functions may result from significant differences in detailed structures and properties of repetitive regions of various types of spidroins. Nevertheless, all CTDs may have a common functional role: dimerization of the CTD doubles the size of silk proteins, reduces the number of chain ends, and thus leads to fewer chain end defects in the fibers formed. Structure and function of C-terminal domain of aciniform spidroin.,Wang S, Huang W, Yang D Biomacromolecules. 2014 Feb 10;15(2):468-77. doi: 10.1021/bm401709v. Epub 2014, Jan 22. PMID:24422432 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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