Structure and function of the C-terminal PABC domain of human poly(A)-binding protein

Acyl-CoA-binding protein (ACBP) is an important protein with a size of about 10 kDa. It has a high binding affinity for C12–C22 acyl-CoA esters and participates in lipid metabolism. ACBP and its family of proteins have been found in all eukaryotes and some prokaryotes. Studies have described the function and structure of ACBP family proteins in mammals (such as humans and mice), plants (such as Oryza sativa, Arabidopsis thaliana, and Hevea brasiliensis) and yeast. However, little information on the structure and function of the proteins in filamentous fungi has been reported. This article concentrates on recent advances in the research of the ACBP family proteins in plants and mammals, especially in yeast, filamentous fungi (such as Monascus ruber and Aspergillus oryzae), and fungal pathogens (Aspergillus flavus, Cryptococcus neoformans). Furthermore, we discuss some problems in the field, summarize the binding characteristics of the ACBP family proteins in filamentous fungi and yeast, and consider the future of ACBP development.

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Structure and function of a novel calcium-binding protein, CaBPc, from cardiac muscle.

The Japanese Journal of Pharmacology ◽

10.1016/s0021-5198(19)38299-x ◽

1991 ◽

Vol 55 ◽

pp. 96

Author(s):

Michiko Naka ◽

Toshiya Sasaki ◽

Hideaki Kise ◽

Isao Tawara ◽

Satoshi Hamaguchi ◽

...

Keyword(s):

Cardiac Muscle ◽

Calcium Binding ◽

Binding Protein ◽

Structure And Function ◽

Calcium Binding Protein ◽

And Function

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Structure and function of lipopolysaccharide binding protein

Science ◽

10.1126/science.2402637 ◽

1990 ◽

Vol 249 (4975) ◽

pp. 1429-1431 ◽

Cited By ~ 1039

Author(s):

R. Schumann ◽

Leong ◽

G. Flaggs ◽

P. Gray ◽

S. Wright ◽

...

Keyword(s):

Binding Protein ◽

Structure And Function ◽

Lipopolysaccharide Binding Protein ◽

And Function ◽

Lipopolysaccharide Binding

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Identification of Avian Corticosteroid-binding Globulin (SerpinA6) Reveals the Molecular Basis of Evolutionary Adaptations in SerpinA6 Structure and Function as a Steroid-binding Protein

Journal of Biological Chemistry ◽

10.1074/jbc.m116.714378 ◽

2016 ◽

Vol 291 (21) ◽

pp. 11300-11312 ◽

Cited By ~ 7

Author(s):

Ganna Vashchenko ◽

Samir Das ◽

Kyung-Mee Moon ◽

Jason C. Rogalski ◽

Matthew D. Taves ◽

...

Keyword(s):

Molecular Basis ◽

Binding Protein ◽

Structure And Function ◽

Corticosteroid Binding Globulin ◽

Steroid Binding ◽

And Function ◽

Steroid Binding Protein

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

PeerJ ◽

10.7717/peerj.4396 ◽

2018 ◽

Vol 6 ◽

pp. e4396 ◽

Cited By ~ 5

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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