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Crystal structure and conformation of the cyclic tetramer of a repeat tripeptide of elastin, cyclo(l-valyl-l-prolylglycyl)4

✍ Scribed by COOK, WILLIAM J. ;TRAPANE, TINA L. ;PRASAD, KARI U.

Book ID: 115098329
Publisher: Wiley (Blackwell Publishing)
Year: 2009
Tongue: English
Weight: 344 KB
Volume: 25
Category: Article
ISSN: 0367-8377
DOI: 10.1111/j.1399-3011.1985.tb02202.x

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✦ Synopsis

X‐ray diffraction data were used to determine the crystal structure of cyclo‐(l‐Val‐l‐Pro‐Gly)~4~, the cyclic tetramer of a repeat tripeptide of elastin. The crystals are monoclinic, space group C2, with a = 29.639(3), b = 7.099(1), c = 20.325 (2) Å, and β = 130.4(4)°. The structure was solved by direct methods and refined by least squares to R = 0.082 for 2603 observed reflections. The cyclic dodecapeptide contains two β(II) turns. Hydrophilic and hydrophobic channels that run parallel to the b axis are formed by the stacking of cyclic peptides on twofold axes.

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