Crystal structure of deltakephalin: a γ‐selective opioid peptide with a novel β‐bend‐like conformation Article

FLIPPEN‐ANDERSON, JL, DESCHAMPS, JR, WARD, KB et al. (1994). Crystal structure of deltakephalin: a γ‐selective opioid peptide with a novel β‐bend‐like conformation . International Journal of Peptide and Protein Research, 44(2), 97-104. 10.1111/j.1399-3011.1994.tb00563.x

cited authors

  • FLIPPEN‐ANDERSON, JL; DESCHAMPS, JR; WARD, KB; GEORGE, C; HOUGHTEN, R

abstract

  • The solid‐state structure of deltakephalin (Tyr‐D Thr‐Gly‐Phc‐Leu‐Thr) has been determined by single‐crystal X‐ray diffraction. Deltakephalin (DTLET) is a synthetic opioid peptide which differs from enkephalin in that a d‐Thr has been substituted for Gly2 and a sixth residue, l‐Thr, has been added. Clear colorless plates obtained using vapor diffusion and macro‐seeding crystallization techniques were monoclinic; space group C2 with u = 27.389(5), b = 9.205(2), c = 16.788(2) Å, β= 98.87(2) ˚ and V= 4181.4(14) Å3. The asymmetric unit contained one molecule of DTLET and six molecules of water, giving a calculated density of 1.28 g cm−3. The crystal structure revealed that DTLET has a pseudo type I'β‐bend which is stabilized by an intramolecular side‐chain to backbone hydrogen bond. This is the first reported observation of a pseudo β‐bend conformation in a solid‐sate structure of an enkephalin analog. Copyright © 1994, Wiley Blackwell. All rights reserved

authors

publication date

  • January 1, 1994

published in

Digital Object Identifier (DOI)

start page

  • 97

end page

  • 104

volume

  • 44

issue

  • 2