2khm

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{{Seed}}
 
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[[Image:2khm.jpg|left|200px]]
 
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==Structure of the C-terminal non-repetitive domain of the spider dragline silk protein ADF-3==
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The line below this paragraph, containing "STRUCTURE_2khm", creates the "Structure Box" on the page.
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<StructureSection load='2khm' size='340' side='right'caption='[[2khm]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2khm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Araneus_diadematus Araneus diadematus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2KHM FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 21 models</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2khm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2khm OCA], [https://pdbe.org/2khm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2khm RCSB], [https://www.ebi.ac.uk/pdbsum/2khm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2khm ProSAT]</span></td></tr>
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{{STRUCTURE_2khm| PDB=2khm | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q16987_ARADI Q16987_ARADI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kh/2khm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A 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.
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===The carboxy-terminal non-repetitive domain of a spider dragline silk protein regulates nucleation of silk assembly===
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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<ref>PMID:20463741</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2khm" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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2KHM is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Araneus_diadematus Araneus diadematus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KHM OCA].
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*[[Fibroins|Fibroins]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Araneus diadematus]]
[[Category: Araneus diadematus]]
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[[Category: Coles, M.]]
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[[Category: Large Structures]]
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[[Category: Eisoldt, L.]]
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[[Category: Coles M]]
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[[Category: Hagn, F X.]]
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[[Category: Eisoldt L]]
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[[Category: Hardy, J.]]
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[[Category: Hagn FX]]
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[[Category: Kessler, H.]]
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[[Category: Hardy JG]]
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[[Category: Scheibel, T.]]
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[[Category: Kessler H]]
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[[Category: Vendrely, C.]]
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[[Category: Scheibel T]]
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[[Category: Alpha helix]]
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[[Category: Vendrely C]]
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[[Category: Homodimer]]
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[[Category: Structural protein]]
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[[Category: Swapped]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 14 09:46:05 2010''
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Current revision

Structure of the C-terminal non-repetitive domain of the spider dragline silk protein ADF-3

PDB ID 2khm

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