Study of Membrane-Induced Conformations of Substance P: Detection of Extended Polyproline II Helix Conformation

2011 ◽  
Vol 115 (13) ◽  
pp. 3622-3631 ◽  
Author(s):  
Arash Foroutan ◽  
Tzvetana Lazarova ◽  
Esteve Padrós
Keyword(s):  
Substance P ◽  
Polyproline Ii ◽  
Polyproline Ii Helix ◽  
Helix Conformation

scholarly journals Polyproline II Helix Conformation in a Proline-Rich Environment: A Theoretical Study

2004 ◽  
Vol 86 (2) ◽  
pp. 731-742 ◽  
Author(s):  
Jorge A. Vila ◽  
Héctor A. Baldoni ◽  
Daniel R. Ripoll ◽  
Avijit Ghosh ◽  
Harold A. Scheraga
Keyword(s):  
Theoretical Study ◽  
Polyproline Ii ◽  
Polyproline Ii Helix ◽  
Helix Conformation

scholarly journals Allosteric Modulation of the Dopamine D2Receptor by Pro-Leu-Gly-NH2Peptidomimetics Constrained in Either a Polyproline II Helix or a Type II β-Turn Conformation

2009 ◽  
Vol 52 (7) ◽  
pp. 2043-2051 ◽  
Author(s):  
Bhooma Raghavan ◽  
Kevin J. Skoblenick ◽  
Swapna Bhagwanth ◽  
Niran Argintaru ◽  
Ram K. Mishra ◽  
...  
Keyword(s):  
Allosteric Modulation ◽  
Type Ii ◽  
Polyproline Ii ◽  
Polyproline Ii Helix

Polyproline II Helix Is a Key Structural Motif of the Elastic PEVK Segment of Titin

Biochemistry ◽  
2001 ◽  
Vol 40 (12) ◽  
pp. 3427-3438 ◽  
Author(s):  
Kan Ma ◽  
Lou-sing Kan ◽  
Kuan Wang
Keyword(s):  
Structural Motif ◽  
Polyproline Ii ◽  
Polyproline Ii Helix

scholarly journals Left-handed polyproline-II helix revisited: proteins causing proteopathies

2016 ◽  
Vol 35 (12) ◽  
pp. 2701-2713 ◽  
Author(s):  
Alexei A. Adzhubei ◽  
Anastasia A. Anashkina ◽  
Alexander A. Makarov
Keyword(s):  
Left Handed ◽  
Polyproline Ii ◽  
Polyproline Ii Helix

Polyproline-II Helix in Proteins: Structure and Function

2013 ◽  
Vol 425 (12) ◽  
pp. 2100-2132 ◽  
Author(s):  
Alexei A. Adzhubei ◽  
Michael J.E. Sternberg ◽  
Alexander A. Makarov
Keyword(s):  
Structure And Function ◽  
Polyproline Ii ◽  
Polyproline Ii Helix ◽  
And Function

scholarly journals Microsecond and nanosecond polyproline II helix formation in aqueous nanodrops measured by mass spectrometry

2016 ◽  
Vol 52 (82) ◽  
pp. 12218-12221 ◽  
Author(s):  
Daniel N. Mortensen ◽  
Evan R. Williams
Keyword(s):  
Mass Spectrometry ◽  
Time Constants ◽  
Rapid Mixing ◽  
Helix Formation ◽  
Polyproline Ii ◽  
Polyproline Ii Helix

The 1.5 μs and <400 ns time constants for the formation of polyproline II helix structures in 21 and 16 residue peptides, respectively, are measured using rapid mixing from theta-glass emitters coupled with mass spectrometry.

O2-05-04: Hyperphosphorylation of Tau induces local polyproline II helix in the proline-rich domain

2008 ◽  
Vol 4 ◽  
pp. T141-T142
Author(s):  
Neal J. Zondlo ◽  
Agata A. Bielska ◽  
Aaron E. Lee
Keyword(s):  
Rich Domain ◽  
Polyproline Ii ◽  
Polyproline Ii Helix

scholarly journals The physiological butyrylcholinesterase tetramer is a dimer of dimers stabilized by a superhelical assembly

2018 ◽  
Author(s):  
Miguel Ricardo Leung ◽  
Laura S. van Bezouwen ◽  
Lawrence M. Schopfer ◽  
Joel L. Sussman ◽  
Israel Silman ◽  
...  
Keyword(s):  
Practical Importance ◽  
Residence Times ◽  
Catalytic Domains ◽  
Polyproline Ii ◽  
Cryo Electron Microscopy ◽  
Tetramerization Domain ◽  
Polyproline Ii Helix ◽  
Quaternary Structures ◽  
The Stability ◽  
And Function

AbstractThe quaternary structures of the cholinesterases, acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), are essential for their localisation and function. Of practical importance, BChE is a promising therapeutic candidate for intoxication by organophosphate nerve agents and insecticides, and for detoxification of addictive substances. Efficacy of the recombinant enzyme hinges on its having a long circulatory half-life; this, in turn, depends strongly on its ability to tetramerize. Here, we used cryo-electron microscopy (cryo-EM) to determine the structure of the highly glycosylated native BChE tetramer purified from human plasma at 5.7 Å. Our structure reveals that the BChE tetramer is organised as a staggered dimer of dimers. Tetramerization is mediated by assembly of the C-terminal tryptophan amphiphilic tetramerization (WAT) helices from each subunit as a superhelical assembly around a central anti-parallel polyproline II helix (PRAD). The catalytic domains within a dimer are asymmetrically linked to the WAT/PRAD. In the resulting arrangement, the tetramerization domain is largely shielded by the catalytic domains, which may contribute to the stability of the HuBChE tetramer. Our cryo-EM structure reveals the basis for assembly of the physiological tetramers, and has implications for the therapeutic applications of HuBChE. This mode of tetramerization is seen only in the cholinesterases, and may provide a promising template for designing other proteins with improved circulatory residence times.

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