3ipn | pdb_00003ipn

Crystal Structure of fluorine and methyl modified collagen: (mepFlpgly)7

spinqualitylabelsall models 3ipn, resolution 1.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ipn is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.21Å Ligands: CO3, FP9, MP8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Collagen 3D structures

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