scholarly journals Frontispiece: Structure and Function of Human Tyrosinase and Tyrosinase-Related Proteins

2018 ◽  
Vol 24 (1) ◽  
Author(s):  
Xuelei Lai ◽  
Harry J. Wichers ◽  
Montserrat Soler-Lopez ◽  
Bauke W. Dijkstra
Keyword(s):  
Structure And Function ◽  
And Function ◽  
Related Proteins ◽  
Human Tyrosinase

scholarly journals Structure and Function of Human Tyrosinase and Tyrosinase-Related Proteins

2017 ◽  
Vol 24 (1) ◽  
pp. 47-55 ◽  
Author(s):  
Xuelei Lai ◽  
Harry J. Wichers ◽  
Montserrat Soler-Lopez ◽  
Bauke W. Dijkstra
Keyword(s):  
Structure And Function ◽  
And Function ◽  
Related Proteins ◽  
Human Tyrosinase

scholarly journals Conserved Structure and Function in the Granulysin and NK-Lysin Peptide Family

2005 ◽  
Vol 73 (10) ◽  
pp. 6332-6339 ◽  
Author(s):  
Charlotte M. A. Linde ◽  
Susanna Grundström ◽  
Erik Nordling ◽  
Essam Refai ◽  
Patrick J. Brennan ◽  
...  
Keyword(s):  
Mycobacterium Smegmatis ◽  
Three Dimensional ◽  
Antimycobacterial Activity ◽  
Structure And Function ◽  
Loop Structure ◽  
E Coli ◽  
Short Loop ◽  
Peptide Family ◽  
And Function ◽  
Related Proteins

ABSTRACT Granulysin and NK-lysin are homologous bactericidal proteins with a moderate residue identity (35%), both of which have antimycobacterial activity. Short loop peptides derived from the antimycobacterial domains of granulysin, NK-lysin, and a putative chicken NK-lysin were examined and shown to have comparable antimycobacterial but variable Escherichia coli activities. The known structure of the NK-lysin loop peptide was used to predict the structure of the equivalent peptides of granulysin and chicken NK-lysin by homology modeling. The last two adopted a secondary structure almost identical to that of NK-lysin. All three peptides form very similar three-dimensional (3-D) architectures in which the important basic residues assume the same positions in space. The basic residues in granulysin are arginine, while those in NK-lysin and chicken NK-lysin are a mixture of arginine and lysine. We altered the ratio of arginine to lysine in the granulysin fragment to examine the importance of basic residues for antimycobacterial activity. The alteration of the amino acids reduced the activity against E. coli to a larger extent than that against Mycobacterium smegmatis. In granulysin, the arginines in the loop structure are not crucial for antimycobacterial activity but are important for cytotoxicity. We suggest that the antibacterial domains of the related proteins granulysin, NK-lysin, and chicken NK-lysin have conserved their 3-D structure and their function against mycobacteria.

Structure and Function in Dipeptidyl Peptidase IV and Related Proteins

2006 ◽  
pp. 45-54 ◽  
Author(s):  
Mark D. Gorrell ◽  
Xin M. Wang ◽  
Joohong Park ◽  
Katerina Ajami ◽  
Denise Ming Tse Yu ◽  
...  
Keyword(s):  
Dipeptidyl Peptidase ◽  
Structure And Function ◽  
Dipeptidyl Peptidase Iv ◽  
And Function ◽  
Related Proteins

scholarly journals Archaeal MCM Proteins as an Analog for the Eukaryotic Mcm2–7 Helicase to Reveal Essential Features of Structure and Function

Archaea ◽  
2015 ◽  
Vol 2015 ◽  
pp. 1-14 ◽  
Author(s):  
Justin M. Miller ◽  
Eric J. Enemark
Keyword(s):  
Replication Fork ◽  
Structure And Function ◽  
Replicative Helicase ◽  
The Core ◽  
Mcm Helicase ◽  
Mcm Proteins ◽  
And Function ◽  
Related Proteins

In eukaryotes, the replicative helicase is the large multisubunit CMG complex consisting of the Mcm2–7 hexameric ring, Cdc45, and the tetrameric GINS complex. The Mcm2–7 ring assembles from six different, related proteins and forms the core of this complex. In archaea, a homologous MCM hexameric ring functions as the replicative helicase at the replication fork. Archaeal MCM proteins form thermostable homohexamers, facilitating their use as models of the eukaryotic Mcm2–7 helicase. Here we review archaeal MCM helicase structure and function and how the archaeal findings relate to the eukaryotic Mcm2–7 ring.

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