2mab
From Proteopedia
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| - | ''' | + | ==Untangling the Solution Structure of C-Terminal Domain of Aciniform Spidroin== |
| + | <StructureSection load='2mab' size='340' side='right' caption='[[2mab]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mab]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nephila_antipodiana Nephila antipodiana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MAB FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mab OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mab RCSB], [http://www.ebi.ac.uk/pdbsum/2mab PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:24422432</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Nephila antipodiana]] | ||
| + | [[Category: Wang, S.]] | ||
| + | [[Category: Yang, D.]] | ||
| + | [[Category: Aciniform spidroin]] | ||
| + | [[Category: C-terminal domain]] | ||
| + | [[Category: Spider silk protein]] | ||
| + | [[Category: Structural protein]] | ||
Revision as of 11:41, 18 May 2014
Untangling the Solution Structure of C-Terminal Domain of Aciniform Spidroin
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