Literature DB >> 2172962

Acid helix-turn activator motif.

Q L Zhu1, T F Smith, R H Lathrop, J Figge.   

Abstract

A common sequence/structural motif pattern has been identified within the steroid/thyroid hormone receptors and other transcriptional activators using a new massively parallel symbolic learning assistant computer system. The pattern appears nearly diagnostic of transcription activation, including relative activation strength, among nuclear and DNA-binding prokaryotic proteins. In cases where mutation/deletion/chimeric studies have identified the activation domain, the pattern matches within that domain. These facts and the nature of the pattern itself strongly support the idea that the patterned domain is directly involved in a protein-protein transcription activation interaction.

Mesh:

Substances:

Year:  1990        PMID: 2172962     DOI: 10.1002/prot.340080205

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  4 in total

1.  The binding domain structure of retinoblastoma-binding proteins.

Authors:  J Figge; K Breese; S Vajda; Q L Zhu; L Eisele; T T Andersen; R MacColl; T Friedrich; T F Smith
Journal:  Protein Sci       Date:  1993-02       Impact factor: 6.725

2.  Pattern of aromatic and hydrophobic amino acids critical for one of two subdomains of the VP16 transcriptional activator.

Authors:  J L Regier; F Shen; S J Triezenberg
Journal:  Proc Natl Acad Sci U S A       Date:  1993-02-01       Impact factor: 11.205

3.  Homopolymer length variation in the Drosophila gene mastermind.

Authors:  S J Newfeld; A T Schmid; B Yedvobnick
Journal:  J Mol Evol       Date:  1993-11       Impact factor: 2.395

4.  Interspecific comparison of Drosophila serendipity delta and beta: multimodular structure of these C2H2 zinc finger proteins.

Authors:  P Ferrer; M Crozatier; C Salles; A Vincent
Journal:  J Mol Evol       Date:  1994-03       Impact factor: 2.395

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.