Crystallization and preliminary X-ray diffraction analysis of FKBP12 complexed with a novel neurotrophic ligand

Pengyun Li; Liwei Wang; Yi Ding; Beili Wu; Cuiling Shu; Aihua Nie; Song Li; Beifen Shen; Zihe Rao

doi:10.2174/0929866023408517

Crystallization and preliminary X-ray diffraction analysis of FKBP12 complexed with a novel neurotrophic ligand

Protein Pept Lett. 2002 Oct;9(5):459-63. doi: 10.2174/0929866023408517.

Authors

Pengyun Li¹, Liwei Wang, Yi Ding, Beili Wu, Cuiling Shu, Aihua Nie, Song Li, Beifen Shen, Zihe Rao

Affiliation

¹ Laboratory of Structural Biology, Department of Biological Science and Technology & MOE Laboratory of Protein Science, Tsinghua University, Beijing 100084, China.

PMID: 12370035
DOI: 10.2174/0929866023408517

Abstract

A novel neurotrophic ligand, (3R)-4-(p-Toluenesulfonyl)-1,4-thiazane-3-carboxylic acid-L-Leucine ethyl ester, has been complexed with FKBP12 and crystallized using the hanging-drop vapor-diffusion method. Crystals belong to P2(1) space group, with unit cell parameters a=41.2, b=29.6, c=41.5 A, beta=114.0 degrees. The crystals diffract to 1.8 A resolution limit.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallography, X-Ray
Humans
Ligands
Tacrolimus Binding Protein 1A / chemistry*
Tacrolimus Binding Protein 1A / isolation & purification
Tacrolimus Binding Protein 1A / metabolism

Substances

Ligands
Tacrolimus Binding Protein 1A