4m6a: Difference between revisions
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New page: '''Unreleased structure''' The entry 4m6a is ON HOLD Authors: Luo, J., Teplyakov, A., Obmolova, G., Malia, T.J., Chan, W., Jocobs, S.A., O'Neil,K.T., Gilliland, G.L. Description: N-Ter... |
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==N-Terminal beta-Strand Swapping in a Consensus Derived Alternative Scaffold Driven by Stabilizing Hydrophobic Interactions== | |||
<StructureSection load='4m6a' size='340' side='right'caption='[[4m6a]], [[Resolution|resolution]] 2.71Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4m6a]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M6A FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.71Å</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=4m6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m6a OCA], [https://pdbe.org/4m6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m6a RCSB], [https://www.ebi.ac.uk/pdbsum/4m6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m6a ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of an N-terminal beta-strand-swapped consensus-derived tenascin FN3 alternative scaffold has been determined. A comparison with the unswapped structure reveals that the side chain of residue F88 orients differently and packs more tightly with the hydrophobic core of the domain. Dimer formation also results in the burial of a hydrophobic patch on the surface of the domain. Thus, it appears that tighter packing of F88 in the hydrophobic core and burial of surface hydrophobicity provide the driving forces for the N-terminal beta-strand swapping, leading to the formation of a stable compact dimer. Proteins 2014. (c) 2014 Wiley Periodicals, Inc. | |||
N-terminal beta-strand swapping in a consensus-derived alternative scaffold driven by stabilizing hydrophobic interactions.,Luo J, Teplyakov A, Obmolova G, Malia TJ, Chan W, Jacobs SA, O'Neil KT, Gilliland GL Proteins. 2014 Jan 27. doi: 10.1002/prot.24517. PMID:24464739<ref>PMID:24464739</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4m6a" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Chan W]] | |||
[[Category: Gilliland GL]] | |||
[[Category: Jocobs SA]] | |||
[[Category: Luo J]] | |||
[[Category: Malia TJ]] | |||
[[Category: O'neil KT]] | |||
[[Category: Obmolova G]] | |||
[[Category: Teplyakov A]] | |||
Latest revision as of 19:32, 20 September 2023
N-Terminal beta-Strand Swapping in a Consensus Derived Alternative Scaffold Driven by Stabilizing Hydrophobic InteractionsN-Terminal beta-Strand Swapping in a Consensus Derived Alternative Scaffold Driven by Stabilizing Hydrophobic Interactions
Structural highlights
Publication Abstract from PubMedThe crystal structure of an N-terminal beta-strand-swapped consensus-derived tenascin FN3 alternative scaffold has been determined. A comparison with the unswapped structure reveals that the side chain of residue F88 orients differently and packs more tightly with the hydrophobic core of the domain. Dimer formation also results in the burial of a hydrophobic patch on the surface of the domain. Thus, it appears that tighter packing of F88 in the hydrophobic core and burial of surface hydrophobicity provide the driving forces for the N-terminal beta-strand swapping, leading to the formation of a stable compact dimer. Proteins 2014. (c) 2014 Wiley Periodicals, Inc. N-terminal beta-strand swapping in a consensus-derived alternative scaffold driven by stabilizing hydrophobic interactions.,Luo J, Teplyakov A, Obmolova G, Malia TJ, Chan W, Jacobs SA, O'Neil KT, Gilliland GL Proteins. 2014 Jan 27. doi: 10.1002/prot.24517. PMID:24464739[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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