2drx
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(New page: 200px<br /><applet load="2drx" size="350" color="white" frame="true" align="right" spinBox="true" caption="2drx, resolution 1.40Å" /> '''Structure Analysis o...)
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Revision as of 13:09, 23 January 2008
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Structure Analysis of (POG)4-(LOG)2-(POG)4
Overview
Single crystal structures of host-guest peptides, (Pro-Hyp-Gly)(4)-Leu-Hyp-Gly-(Pro-Hyp-Gly)(5) (LOG1) and (Pro-Hyp-Gly)(4)-, (Leu-Hyp-Gly)(2)-(Pro-Hyp-Gly)(4) (LOG2), have been determined at 1.6 A, and 1.4 A resolution, respectively. In these crystals, the side chain, conformations of the Leu residues were (+)gauche-trans. This, conformational preference for the Leu side chain in the Leu-Hyp-Gly, sequence was explained by stereochemical considerations together with, statistical analysis of PDB data. In the (+)gauche-trans conformation, the, Leu side chain can protrude along the radial direction of the rod-like, triple-helical molecule. One strong hydrophobic interaction of the Leu, residue was observed between adjacent molecules in the LOG2 crystal., Because the Leu-Hyp-Gly sequence is one of the most frequently occurring, triplets in Type I collagen, this strong hydrophobic interaction can be, expected in a fibrillar structure of native collagen. All the Leu residues, in the asymmetric unit of the LOG1 and LOG2 crystals had water molecules, hydrogen bonded to their NH. These water molecules made three additional, hydrogen bonds with the Hyp OH, the Gly O==C, and a water molecule in the, 2(nd) hydration shell, forming a tetrahedral coordination of hydrogen, bonds, which allows a smaller mean-square displacement factor of this, water oxygen atom than those of other water molecules. These hydrogen, bonds stabilize the molecular and packing structures by forming one, O==C(Gly) --- W --- OH(Hyp) intra-molecular linkage and two NH(Leu) --- W, --- O==C(Gly) and NH(Leu) --- W --- OH(Hyp) inter-molecular linkages. (c), 2007 Wiley Periodicals, Inc. Biopolymers, 2007.
About this Structure
2DRX is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Unique side chain conformation of a leu residue in a triple-helical structure., Okuyama K, Narita H, Kawaguchi T, Noguchi K, Tanaka Y, Nishino N, Biopolymers. 2007 Mar 20;. PMID:17373653
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