7but
From Proteopedia
(Difference between revisions)
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<StructureSection load='7but' size='340' side='right'caption='[[7but]]' scene=''> | <StructureSection load='7but' size='340' side='right'caption='[[7but]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>[[7but]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichonephila_antipodiana Trichonephila antipodiana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BUT FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7but FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7but OCA], [https://pdbe.org/7but PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7but RCSB], [https://www.ebi.ac.uk/pdbsum/7but PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7but ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Spider silk is self-assembled from water-soluble silk proteins through changes in the environment, including pH, salt concentrations, and shear force. The N-terminal domains of major and minor ampullate silk proteins have been found to play an important role in the assembly process through salt- and pH-dependent dimerization. Here, we identified the sequences of the N-terminal domains of aciniform silk protein (AcSpN) and major ampullate silk protein (MaSpN) from Nephila antipodiana (NA). Different from MaSpN, our biophysical characterization indicated that AcSpN assembles to form large oligomers, instead of a dimer, upon condition changes from neutral to acidic pH and/or from a high to low salt concentration. Our structural studies, by nuclear magnetic resonance spectroscopy and homology modelling, revealed that AcSpN and MaSpN monomers adopt similar overall structures, but have very different charge distributions contributing to the differential self-association features. The intermolecular interaction interfaces for AcSp oligomers were identified using hydrogen-deuterium exchange mass spectrometry and mutagenesis. On the basis of the monomeric structure and identified interfaces, the oligomeric structures of AcSpN were modelled. The structural information obtained will facilitate an understanding of silk fiber formation mechanisms for aciniform silk protein. | ||
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| + | Structural Basis of Oligomerization of N-Terminal Domain of Spider Aciniform Silk Protein.,Chakraborty R, Fan JS, Lai CC, Raghuvamsi PV, Chee PX, Anand GS, Yang D Int J Mol Sci. 2020 Jun 23;21(12). pii: ijms21124466. doi: 10.3390/ijms21124466. PMID:32586030<ref>PMID:32586030</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7but" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Trichonephila antipodiana]] | ||
[[Category: Fan JS]] | [[Category: Fan JS]] | ||
[[Category: Yang DW]] | [[Category: Yang DW]] | ||
Revision as of 11:11, 14 June 2023
N-terminal domain (NTD) Solution structure of aciniform spidroin (AcSpN) from Nephila antipodiana.
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