scholarly journals 1P115 Crystal structure of the MgtE Mg^ transporter(Membrane proteins,Oral Presentations)

2007 ◽  
Vol 47 (supplement) ◽  
pp. S52
Author(s):  
Motoyuki Hattori ◽  
Yoshiki Tanaka ◽  
Shuya Fukai ◽  
Ryuichiro Ishitani ◽  
Osamu Nureki
Keyword(s):  
Crystal Structure ◽  
Membrane Proteins ◽  
Oral Presentations

scholarly journals 1P110 2D-crystallization of bovine heart NADH-ubiquinone oxidoreductase(Membrane proteins,Oral Presentations)

2007 ◽  
Vol 47 (supplement) ◽  
pp. S51
Author(s):  
Satoko Amano ◽  
Masakazu Moriyama ◽  
Yumiko Nakashima ◽  
Kyoko Shinzawa-Itoh ◽  
Christoph Gerle ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Ubiquinone Oxidoreductase ◽  
Bovine Heart ◽  
Nadh Ubiquinone Oxidoreductase ◽  
Oral Presentations

scholarly journals Hydrophilic microenvironment required for the channel-independent insertase function of YidC protein

2015 ◽  
Vol 112 (16) ◽  
pp. 5063-5068 ◽  
Author(s):  
Naomi Shimokawa-Chiba ◽  
Kaoru Kumazaki ◽  
Tomoya Tsukazaki ◽  
Osamu Nureki ◽  
Koreaki Ito ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Bacillus Subtilis ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Protein Translocation ◽  
Cavity Surface ◽  
Energetic Costs ◽  
Protein Insertion ◽  
Membrane Protein Insertion ◽  
Alternative Sites

The recently solved crystal structure of YidC protein suggests that it mediates membrane protein insertion by means of an intramembrane cavity rather than a transmembrane (TM) pore. This concept of protein translocation prompted us to characterize the native, membrane-integrated state of YidC with respect to the hydropathic nature of its TM region. Here, we show that the cavity-forming region of the stage III sporulation protein J (SpoIIIJ), a YidC homolog, is indeed open to the aqueous milieu of the Bacillus subtilis cells and that the overall hydrophilicity of the cavity, along with the presence of an Arg residue on several alternative sites of the cavity surface, is functionally important. We propose that YidC functions as a proteinaceous amphiphile that interacts with newly synthesized membrane proteins and reduces energetic costs of their membrane traversal.

scholarly journals Druggability analysis of membrane proteins by DoGSiteScorer

2017 ◽  
Author(s):  
Ning Zhang ◽  
Daiwei Li
Keyword(s):  
Crystal Structure ◽  
Membrane Proteins ◽  
Virus Entry ◽  
P2y12 Receptor ◽  
Ligand Complex ◽  
Cardiac Muscle Cells ◽  
Receptor Ligand ◽  
Binding Pockets ◽  
Hiv 1 ◽  
Grid Based

Membrane proteins are the most medicinally important yet to be fully exploited pharmaceutical targets. Here druggability analyses are conducted on three different membrane proteins, namely, the human P2Y12 receptor, glycoprotein-41 that mediates the HIV-1 virus entry and membrane fusion, and phospholamban that regulates the Ca2+ pump in cardiac muscle cells. DoGSiteScorer, a grid-based bioinfromatic technology, is able to identify the binding pockets of all three membrane proteins, and the results were in great agreements with the available crystal structure of P2Y12 receptor-ligand complex. This druggability analysis is especially helpful in cases where the crystal structures of membrane protein-ligand complexes are still difficult to obtain. Better understanding of the druggable pockets of membrane proteins also requires including the membrane environment.

scholarly journals Druggability analysis of membrane proteins by DoGSiteScorer

2017 ◽  
Author(s):  
Ning Zhang ◽  
Daiwei Li
Keyword(s):  
Crystal Structure ◽  
Membrane Proteins ◽  
Virus Entry ◽  
P2y12 Receptor ◽  
Ligand Complex ◽  
Cardiac Muscle Cells ◽  
Receptor Ligand ◽  
Binding Pockets ◽  
Hiv 1 ◽  
Grid Based

Membrane proteins are the most medicinally important yet to be fully exploited pharmaceutical targets. Here druggability analyses are conducted on three different membrane proteins, namely, the human P2Y12 receptor, glycoprotein-41 that mediates the HIV-1 virus entry and membrane fusion, and phospholamban that regulates the Ca2+ pump in cardiac muscle cells. DoGSiteScorer, a grid-based bioinfromatic technology, is able to identify the binding pockets of all three membrane proteins, and the results were in great agreements with the available crystal structure of P2Y12 receptor-ligand complex. This druggability analysis is especially helpful in cases where the crystal structures of membrane protein-ligand complexes are still difficult to obtain. Better understanding of the druggable pockets of membrane proteins also requires including the membrane environment.

scholarly journals 1P091 Dissociation of Halorhodopsin Trimer in Detergent System(Membrane proteins,Oral Presentations)

2007 ◽  
Vol 47 (supplement) ◽  
pp. S46
Author(s):  
Takashi Tsukamoto ◽  
Takanori Sasaki ◽  
Megumi Kubo ◽  
Masakatsu Kamiya ◽  
Tomoyasu Aizawa ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Detergent System ◽  
Oral Presentations
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