scholarly journals Beta Strand

2020 ◽  
Author(s):  
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1990 ◽  
Vol 194 (1) ◽  
pp. 51-56 ◽  
Author(s):  
Andreas J. SCHULZE ◽  
Ulrich BAUMANN ◽  
Siegward KNOF ◽  
Ernst JAEGER ◽  
Robert HUBER ◽  
...  

2020 ◽  
Author(s):  
Lanyue Cui ◽  
Jiaoyu He ◽  
Junhang Deng ◽  
Zhilin Song ◽  
Qiufu Li ◽  
...  

Abstract Background: Steroidogenic factor 1 (SF1, NR5A1) is a key transcriptional regulator involved in the hypothalamic-pituitary-steroidogenic organ development. Recently, heterozygous mutations in NR5A1 were found may contribute to the male infertility aetiology. Here, we investigated the association of polymorphisms in NR5A1 gene with azoospermic men in Sichuan, China. Methods: We have performed the NR5A1 gene direct secquencing in a cohort of 102 well-characterised idiopathic Chinese azoospermic infertile men versus 103 fertile men, who were selected by Semen analysis, Karyotype analysis and Y-chromosomal AZF deletion screening. We identified two previously described missense p. Results: Gly146Ala (rs1110061; c.437 G>C) and p.Arg313His (c.938G>A), and the frequency of 437C ( [OR] 1.846, 95% [CI] 1.227-2.778, P=0.003), 437GC (OR =1.884 , 95% CI =1.037-3.422 , P =0.037 ) and 437CC (OR =3.586 , 95% CI =1.397-9.206 , P =0.006 ) were found to be increased significantly in azoospermic patients while no mutations in control .Moreover, one novel heterozygous p.Ser322ILe (c.965 G >A) missense mutation was found in 8 patients which highly conserved serine to isoleucine shown in the Beta strand domain on SF-1 protein. Conclusions: This is the first study, according to our knowledge, to investigate the association between the polymorphisms of NR5A1 gene and azoospermic men in China, and these results suggest that the Gly146Ala polymorphism may be a susceptibility factor for the azoospermic men in Sichuan, China.


2019 ◽  
Vol 141 (11) ◽  
pp. 4526-4530 ◽  
Author(s):  
Qiang Zhang ◽  
Antonino Schepis ◽  
Hai Huang ◽  
Junjiao Yang ◽  
Wen Ma ◽  
...  
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2017 ◽  
Vol 13 (4) ◽  
Author(s):  
Dawid Dułak ◽  
Mateusz Banach ◽  
Zdzisław Wiśniowski ◽  
Leszek Konieczny ◽  
Irena Roterman

AbstractThe mechanism of specific ligand binding by proteins is discussed using the PDZ domain complexing the pentapeptide. This process is critical for clustering the membrane ion channel. The traditional model based on the Beta-sheet extension by complexed pentapeptide is interpreted as a hydrophobic core extension supported by additional Beta-strand generated by complexed pentapeptide. The explanation is based on the fuzzy oil drop model applied to the crystal structure of PDZ-pentapeptide.


Author(s):  
Roman Laskowski ◽  
Tjaart de Beer
Keyword(s):  

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