Sandbox Reserved 350: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 21: | Line 21: | ||
'''The FVa-C2''', which is classified as a '''distorted jelly-roll β-barrel motif''', is compossed of e'''ight major antiparallel strands''' arranged into two '''β-sheets of five and three strands''' packed against one another. | '''The FVa-C2''', which is classified as a '''distorted jelly-roll β-barrel motif''', is compossed of e'''ight major antiparallel strands''' arranged into two '''β-sheets of five and three strands''' packed against one another. | ||
<br /> | <br /> | ||
Salt bridges located within the "upper" segment (Asp61-Arg134)'''--Fig2.--''' and the "lower" segment considered basic, due to the XXX '''basic residues''' present in number and alkalinity?. Both together.. | |||
<br /> | |||
'''The Three Loops''' | |||
<br /> | |||
(1)-Ser21-Trp31 | |||
<br /> | |||
(2)-Asn39-Asn45 | |||
<br /> | |||
(3)-Gly75-Tyr84 | |||
All are described by ''Authors of the paper'' to protrude like spikes from the bottom of the barrel in monomeric FVa-C2. It is also worth noting that spike (1) & spike (3) are separated by β-hairpin structures and spike (2) is described as a wider irregularly loop comparatively. These three loops extending from the C2 domain, are all linked to each other, and to '''three shorter loops''' by an intricate '''H-bonding network''' which extends to residues at the bottom of the β-barrel. | |||
The overall Barrel structure is closed at the top and bottom by '''three''' and '''two''' straight segments, giving it an '''overall spherical shape''' with a flattened upper surface. | The overall Barrel structure is closed at the top and bottom by '''three''' and '''two''' straight segments, giving it an '''overall spherical shape''' with a flattened upper surface. | ||
<br /> | <br /> | ||
