title: Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the human TLE1 Q domain.
abstract: Human transducin-like enhancer of split 1 (TLE1) plays crucial roles in a number of developmental processes and is involved in pathogenesis of malignancy tumors. The N-terminal glutamine-rich domain (Q domain) of TLE1 mediates its tetramerization and interactions with different DNA-binding transcription factors to regulate Notch and Wnt signaling pathways. To better understand the molecular mechanism of TLE1's functions in these pathways, we cloned, purified, and crystallized the TLE1 Q domain (TLE1-Q). The crystals belong to space group C222(1), with the complete diffraction data of the native and Se-Met TLE1-Q collected to 3.5 and 4.1 Å resolutions, respectively. The phasing-solving and model building are in progress.
authors.affiliation: Department of Thoracic and Cardiovascular Surgery, Changzheng Hospital, Second Military Medical University, Shanghai, China.
authors.forename: Su
authors.initials: S
authors.lastname: Wang
authors.forename: Jiamu
authors.initials: J
authors.lastname: Du
authors.forename: Hua
authors.initials: H
authors.lastname: Tang
authors.forename: Xinyu
authors.initials: X
authors.lastname: Ding
authors.forename: Manwu
authors.initials: M
authors.lastname: Zha
authors.forename: Zhifei
authors.initials: Z
authors.lastname: Xu
mesh_terms: D002942:Circular Dichroism / Q000295:instrumentation; D003001:Cloning, Molecular / Q000379:methods; D056970:Co-Repressor Proteins; D003460:Crystallization / Q000379:methods*; D006801:Humans; D012097:Repressor Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification*; D014961:X-Ray Diffraction / Q000379:methods*
chemical_list: D056970:Co-Repressor Proteins; D012097:Repressor Proteins; C499043:TLE1 protein, human