3ipn
From Proteopedia
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| - | [[Image:3ipn.png|left|200px]] | ||
| - | + | ==Crystal Structure of fluorine and methyl modified collagen: (mepFlpgly)7== | |
| + | <StructureSection load='3ipn' size='340' side='right'caption='[[3ipn]], [[Resolution|resolution]] 1.21Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ipn]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IPN 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]] 1.21Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FP9:(4R)-4-FLUORO-L-PROLINE'>FP9</scene>, <scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene></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=3ipn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ipn OCA], [https://pdbe.org/3ipn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ipn RCSB], [https://www.ebi.ac.uk/pdbsum/3ipn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ipn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Preorganization is shown to endow a protein with extraordinary conformational stability. This preorganization is achieved by installing side-chain substituents that impose stereoelectronic and steric effects that restrict main-chain torsion angles. Replacing proline residues in (ProProGly)(7) collagen strands with 4-fluoroproline and 4-methylproline leads to the most stable known triple helices, having T ( m ) values that are increased by > 50 degrees C. Differential scanning calorimetry data indicate an entropic basis to the hyperstability, as expected from an origin in preorganization. Structural data at a resolution of 1.21 A reveal a prototypical triple helix with insignificant deviations to its main chain, even though 2/3 of the residues are nonnatural. Thus, preorganization of a main chain by subtle changes to side chains can confer extraordinary conformational stability upon a protein without perturbing its structure. | ||
| - | + | Stereoelectronic and steric effects in side chains preorganize a protein main chain.,Shoulders MD, Satyshur KA, Forest KT, Raines RT Proc Natl Acad Sci U S A. 2010 Jan 12;107(2):559-64. Epub 2009 Dec 31. PMID:20080719<ref>PMID:20080719</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3ipn" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Collagen|Collagen]] | + | *[[Collagen 3D structures|Collagen 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Forest KT]] |
| - | [[Category: | + | [[Category: Raines RT]] |
| - | [[Category: | + | [[Category: Satyshur KA]] |
| - | + | [[Category: Shoulders MD]] | |
| - | + | ||
| - | + | ||
Current revision
Crystal Structure of fluorine and methyl modified collagen: (mepFlpgly)7
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