Literature DB >> 2553124

The use of folding patterns in a multisolution approach of the all-beta protein three-dimensional structure. A beta-roll structure is predicted in the retroviral glycoprotein.

B Busetta1.   

Abstract

An automatic macromolecular modelling package of unknown protein structures was developed using the intimate correlation which appears between the observed X-ray structures and their associated predicted folding patterns. The method can be considered as a generalization of both the combinatorial [1] and the template identification [2,3] approaches which were proposed some years ago, and provide a fast way of selecting 'structural motifs' to build new proteins. As an illustration, the tertiary fold of the all-beta-domain of the retroviral outermembrane glycoprotein is proposed.

Entities:  

Mesh:

Substances:

Year:  1989        PMID: 2553124     DOI: 10.1016/0167-4838(89)90289-6

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Sequence variability of bovine leukemia virus env gene and its relevance to the structure and antigenicity of the glycoproteins.

Authors:  R Z Mamoun; M Morisson; N Rebeyrotte; B Busetta; D Couez; R Kettmann; M Hospital; B Guillemain
Journal:  J Virol       Date:  1990-09       Impact factor: 5.103

2.  Fusion of bovine leukemia virus with target cells monitored by R18 fluorescence and PCR assays.

Authors:  S Zarkik; F Defrise-Quertain; D Portetelle; A Burny; J M Ruysschaert
Journal:  J Virol       Date:  1997-01       Impact factor: 5.103

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.