Three-dimensional structure and function study on the active region in the extracellular ligand-binding domain of human IL-6 receptor

2000 ◽  
Vol 43 (4) ◽  
pp. 425-432
Author(s):  
Yunfang Ren ◽  
Jiannan Feng ◽  
Hong Qu ◽  
Song Li ◽  
Beifen Shen
Keyword(s):  
Active Region ◽  
Ligand Binding ◽  
Three Dimensional ◽  
Structure And Function ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Function Study ◽  
And Function

scholarly journals Impact of genetic variation on three dimensional structure and function of proteins

PLoS ONE ◽  
2017 ◽  
Vol 12 (3) ◽  
pp. e0171355 ◽  
Author(s):  
Roshni Bhattacharya ◽  
Peter W. Rose ◽  
Stephen K. Burley ◽  
Andreas Prlić
Keyword(s):  
Genetic Variation ◽  
Three Dimensional ◽  
Structure And Function ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
And Function

scholarly journals In silicostructural and functional prediction of African swine fever virus protein-B263R reveals features of a TATA-binding protein

PeerJ ◽  
2018 ◽  
Vol 6 ◽  
pp. e4396 ◽  
Author(s):  
Dickson Kinyanyi ◽  
George Obiero ◽  
George F.O. Obiero ◽  
Peris Amwayi ◽  
Stephen Mwaniki ◽  
...  
Keyword(s):  
African Swine Fever Virus ◽  
Binding Protein ◽  
Three Dimensional ◽  
African Swine Fever ◽  
Tata Binding Protein ◽  
Structure And Function ◽  
Fever Virus ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
And Function

African swine fever virus (ASFV) is the etiological agent of ASF, a fatal hemorrhagic fever that affects domestic pigs. There is currently no vaccine against ASFV, making it a significant threat to the pork industry. The ASFV genome sequence has been published; however, about half of ASFV open reading frames have not been characterized in terms of their structure and function despite being essential for our understanding of ASFV pathogenicity. The present study reports the three-dimensional structure and function of uncharacterized protein, pB263R (NP_042780.1), an open reading frame found in all ASFV strains. Sequence-based profiling and hidden Markov model search methods were used to identify remote pB263R homologs. Iterative Threading ASSEmbly Refinement (I-TASSER) was used to model the three-dimensional structure of pB263R. The posterior probability of fold family assignment was calculated using TM-fold, and biological function was assigned using TM-site, RaptorXBinding, Gene Ontology, and TM-align. Our results suggests that pB263R has the features of a TATA-binding protein and is thus likely to be involved in viral gene transcription.

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