3u29

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==Structural insights into charge pair interactions in triple helical proteins==
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<StructureSection load='3u29' size='340' side='right' caption='[[3u29]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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==Crystal Structure of a KGD Collagen Mimetic Peptide at 2.0 A==
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<StructureSection load='3u29' size='340' side='right'caption='[[3u29]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3u29]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U29 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3u29]] is a 6 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=3U29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U29 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene></td></tr>
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</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&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t4f|3t4f]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3u29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u29 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u29 RCSB], [http://www.ebi.ac.uk/pdbsum/3u29 PDBsum]</span></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=3u29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u29 OCA], [https://pdbe.org/3u29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u29 RCSB], [https://www.ebi.ac.uk/pdbsum/3u29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u29 ProSAT]</span></td></tr>
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<table>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The collagen triple helix is the most abundant protein fold in humans. Despite its deceptively simple structure, very little is understood about its folding and fibrillization energy landscape. In this work, using a combination of x-ray crystallography and nuclear magnetic resonance spectroscopy, we carry out a detailed study of stabilizing pair-wise interactions between the positively charged lysine and the negatively charged amino acids aspartate and glutamate. We find important differences in the side chain conformation of amino acids in the crystalline and solution state. Structures from x-ray crystallography may have similarities to the densely packed triple helices of collagen fibers whereas solution NMR structures reveal the simpler interactions of isolated triple helices. In solution, two distinct types of contacts are observed: axial and lateral. Such register-specific interactions are crucial for the understanding of the registration process of collagens and the overall stability of proteins in this family. However, in the crystalline state, there is a significant rearrangement of the side chain conformation allowing for packing interactions between adjacent helices, which suggests that charged amino acids may play a dual role in collagen stabilization and folding, first at the level of triple helical assembly and second during fibril formation.
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Structural insights into charge pair interactions in triple helical collagen-like proteins.,Fallas JA, Dong J, Tao YJ, Hartgerink JD J Biol Chem. 2012 Mar 9;287(11):8039-47. Epub 2011 Dec 17. PMID:22179819<ref>PMID:22179819</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Dong, J.]]
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[[Category: Large Structures]]
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[[Category: Fallas, J A.]]
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[[Category: Synthetic construct]]
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[[Category: Hartgerink, J D.]]
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[[Category: Dong J]]
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[[Category: Tao, Y J.]]
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[[Category: Fallas JA]]
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[[Category: Biosynthetic protein]]
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[[Category: Hartgerink JD]]
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[[Category: Triple helix]]
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[[Category: Miller MD]]
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[[Category: Tao YJ]]

Current revision

Crystal Structure of a KGD Collagen Mimetic Peptide at 2.0 A

PDB ID 3u29

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