2khm: Difference between revisions
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==Structure of the C-terminal non-repetitive domain of the spider dragline silk protein ADF-3== | ==Structure of the C-terminal non-repetitive domain of the spider dragline silk protein ADF-3== | ||
<StructureSection load='2khm' size='340' side='right' caption='[[2khm]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | <StructureSection load='2khm' size='340' side='right' caption='[[2khm]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | ||
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<table><tr><td colspan='2'>[[2khm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aradi Aradi]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KHM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KHM FirstGlance]. <br> | <table><tr><td colspan='2'>[[2khm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aradi Aradi]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KHM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KHM FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADF-3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=45920 ARADI])</td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADF-3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=45920 ARADI])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2khm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2khm OCA], [http://pdbe.org/2khm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2khm RCSB], [http://www.ebi.ac.uk/pdbsum/2khm PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2khm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2khm OCA], [http://pdbe.org/2khm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2khm RCSB], [http://www.ebi.ac.uk/pdbsum/2khm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2khm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kh/2khm_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kh/2khm_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2khm ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2khm" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2khm" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Fibroins|Fibroins]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 14:03, 18 July 2018
Structure of the C-terminal non-repetitive domain of the spider dragline silk protein ADF-3Structure of the C-terminal non-repetitive domain of the spider dragline silk protein ADF-3
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA huge variety of proteins are able to form fibrillar structures, especially at high protein concentrations. Hence, it is surprising that spider silk proteins can be stored in a soluble form at high concentrations and transformed into extremely stable fibres on demand. Silk proteins are reminiscent of amphiphilic block copolymers containing stretches of polyalanine and glycine-rich polar elements forming a repetitive core flanked by highly conserved non-repetitive amino-terminal and carboxy-terminal domains. The N-terminal domain comprises a secretion signal, but further functions remain unassigned. The C-terminal domain was implicated in the control of solubility and fibre formation initiated by changes in ionic composition and mechanical stimuli known to align the repetitive sequence elements and promote beta-sheet formation. However, despite recent structural data, little is known about this remarkable behaviour in molecular detail. Here we present the solution structure of the C-terminal domain of a spider dragline silk protein and provide evidence that the structural state of this domain is essential for controlled switching between the storage and assembly forms of silk proteins. In addition, the C-terminal domain also has a role in the alignment of secondary structural features formed by the repetitive elements in the backbone of spider silk proteins, which is known to be important for the mechanical properties of the fibre. A conserved spider silk domain acts as a molecular switch that controls fibre assembly.,Hagn F, Eisoldt L, Hardy JG, Vendrely C, Coles M, Scheibel T, Kessler H Nature. 2010 May 13;465(7295):239-42. PMID:20463741[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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