scholarly journals Generic GPCR residue numbers – aligning topology maps while minding the gaps

2015 ◽  
Vol 36 (1) ◽  
pp. 22-31 ◽  
Author(s):  
Vignir Isberg ◽  
Chris de Graaf ◽  
Andrea Bortolato ◽  
Vadim Cherezov ◽  
Vsevolod Katritch ◽  
...  
Keyword(s):  
Residue Numbers

Experimental High Speed/Power Ratio ASIC Designs Using Residue Numbers

1990 ◽  
Author(s):  
A. Simoneau ◽  
J. Pizarro ◽  
A. Parker
Keyword(s):  
High Speed ◽  
Power Ratio ◽  
Residue Numbers

Optical adder for residue numbers

1988 ◽  
Vol 46 (2) ◽  
pp. 125-130
Author(s):  
G. Mitterer ◽  
N. Thiemann ◽  
D. Schu�cker ◽  
E. Klement
Keyword(s):  
Residue Numbers

scholarly journals New fungal defensin-like peptides provide evidence for fold change of proteins in evolution

2017 ◽  
Vol 37 (1) ◽  
Author(s):  
Yucheng Wu ◽  
Bin Gao ◽  
Shunyi Zhu
Keyword(s):  
Disulfide Bridge ◽  
Fold Change ◽  
Structure Conservation ◽  
Fold Formation ◽  
Fungal Defensin ◽  
Α Helix ◽  
Residue Numbers ◽  
Evolution Of Proteins ◽  
Multicellular Organisms ◽  
Β Sheet

Defensins containing a consensus cystine framework, Cys[1]…Cys[2]X3Cys[3]…Cys[4]… Cys[5]X1Cys[6] (X, any amino acid except Cys; …, variable residue numbers), are extensively distributed in a variety of multicellular organisms (plants, fungi and invertebrates) and essentially involved in immunity as microbicidal agents. This framework is a prerequisite for forming the cysteine-stabilized α-helix and β-sheet (CSαβ) fold, in which the two invariant motifs, Cys[2]X3Cys[3]/Cys[5]X1Cys[6], are key determinants of fold formation. By using a computational genomics approach, we identified a large superfamily of fungal defensin-like peptides (fDLPs) in the phytopathogenic fungal genus – Zymoseptoria, which includes 132 structurally typical and 63 atypical members. These atypical fDLPs exhibit an altered cystine framework and accompanying fold change associated with their secondary structure elements and disulfide bridge patterns, as identified by protein structure modelling. Despite this, they definitely are homologous with the typical fDLPs in view of their precise gene structure conservation and identical precursor organization. Sequence and structural analyses combined with functional data suggest that most of Zymoseptoria fDLPs might have lost their antimicrobial activity. The present study provides a clear example of fold change in the evolution of proteins and is valuable in establishing remote homology among peptide superfamily members with different folds.

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