7jx4: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:


==Crystal Structure of N-Lysine Peptoid-modified Collagen Triple Helix==
==Crystal Structure of N-Lysine Peptoid-modified Collagen Triple Helix==
<StructureSection load='7jx4' size='340' side='right'caption='[[7jx4]]' scene=''>
<StructureSection load='7jx4' size='340' side='right'caption='[[7jx4]], [[Resolution|resolution]] 0.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JX4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7jx4]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JX4 FirstGlance]. <br>
</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=7jx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jx4 OCA], [https://pdbe.org/7jx4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jx4 RCSB], [https://www.ebi.ac.uk/pdbsum/7jx4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jx4 ProSAT]</span></td></tr>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLY:N-(4-AMINOBUTYL)GLYCINE'>NLY</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6w47|6w47]]</div></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=7jx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jx4 OCA], [https://pdbe.org/7jx4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jx4 RCSB], [https://www.ebi.ac.uk/pdbsum/7jx4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jx4 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
As the only ribosomally encoded N-substituted amino acid, proline promotes distinct secondary protein structures. The high proline content in collagen, the most abundant protein in the human body, is crucial to forming its hallmark structure: the triple-helix. For over five decades, proline has been considered compulsory for synthetic designs aimed at recapitulating collagen's structure and properties. Here we describe that N-substituted glycines (N-glys), also known as peptoid residues, exhibit a general triple-helical propensity similar to or greater than proline, enabling synthesis of stable triple-helical collagen mimetic peptides (CMPs) with unprecedented side chain diversity. Supported by atomic-resolution crystal structures as well as circular dichroism and computational characterizations spanning over 30 N-gly-containing CMPs, we discovered that N-glys stabilize the triple-helix primarily by sterically preorganizing individual chains into the polyproline-II helix. We demonstrated that N-glys with exotic side chains including a "click"-able alkyne and a photosensitive side chain enable CMPs for functional applications including the spatiotemporal control of cell adhesion and migration. The structural principles uncovered in this study open up opportunities for a new generation of collagen-mimetic therapeutics and materials.
Peptoid Residues Make Diverse, Hyperstable Collagen Triple-Helices.,Kessler JL, Kang G, Qin Z, Kang H, Whitby FG, Cheatham TE 3rd, Hill CP, Li Y, Yu SM J Am Chem Soc. 2021 Jul 13. doi: 10.1021/jacs.1c00708. PMID:34255504<ref>PMID:34255504</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7jx4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Hill CP]]
[[Category: Hill, C P]]
[[Category: Kessler JL]]
[[Category: Kessler, J L]]
[[Category: Whitby FG]]
[[Category: Whitby, F G]]
[[Category: Yang LD]]
[[Category: Yang, L D]]
[[Category: Yu MS]]
[[Category: Yu, M S]]
[[Category: Collagen]]
[[Category: Hyper-stable]]
[[Category: Peptoid]]
[[Category: Protein fibril]]
[[Category: Triple helix]]
Retrieved from "https://proteopedia.org/7jx4"