3ipn
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | [[ | + | ==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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IPN FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ipn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ipn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ipn RCSB], [http://www.ebi.ac.uk/pdbsum/3ipn PDBsum]</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> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
==See Also== | ==See Also== | ||
*[[Collagen|Collagen]] | *[[Collagen|Collagen]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: Forest, K T | + | </StructureSection> |
| - | [[Category: Raines, R T | + | [[Category: Forest, K T]] |
| - | [[Category: Satyshur, K A | + | [[Category: Raines, R T]] |
| - | [[Category: Shoulders, M D | + | [[Category: Satyshur, K A]] |
| + | [[Category: Shoulders, M D]] | ||
[[Category: Collagen]] | [[Category: Collagen]] | ||
[[Category: Fluorinated methylated collagen]] | [[Category: Fluorinated methylated collagen]] | ||
[[Category: Nonnatural amino acid]] | [[Category: Nonnatural amino acid]] | ||
[[Category: Structural protein]] | [[Category: Structural protein]] | ||
Revision as of 08:51, 8 December 2014
Crystal Structure of fluorine and methyl modified collagen: (mepFlpgly)7
| |||||||||||
