Sandbox Reserved 350: Difference between revisions
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==Structure== | ==Structure== | ||
The structure of Human Coagulation Factor V (FV) is sculpted from, originates from, precursors from a polypeptide to a A1-A2-B-A3-C1-C2 layout which results in the activated (FVa) protein. | The structure of Human Coagulation Factor V (FV) is sculpted from, originates from, precursors from a translated polypeptide to a A1-A2-B-A3-C1-C2 layout which results in the activated (FVa) protein. | ||
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'''-Heavy A1-A2 Chain''' | '''-Heavy A1-A2 Chain''' | ||
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A second dimeric crystal form of FVa-C2, packed through the free edges of S6 strands, presenting a different Leu104-Val109 | A second dimeric crystal form of FVa-C2, packed through the free edges of S6 strands, presenting a different Leu104-Val109 | ||
loop, suggesting capabilities of adopting a "Closed Form". | loop, suggesting capabilities of adopting a "Closed Form". In contrast to the "Open Form" of FVa-C2; when looking at the loops 1 and 3 are tilted towards the interior of the groove. This change is considered due to a twist around '''Gly28''' cause it to be deformed (pseudo). In general there is a narrowing of the entrance to the shallow inner loop groove, particularly the critical Gln48 carboxamide; Took place due form the concerted tilting/ "twisting" of the main chain atoms, shifting up to ~7Å and a 12Å displacement of the Trp27 moiety-->shifting closer to the other other two loops. Once shifted closer, the groove seen in the '''Open Form''' is covered by a hydrophobic ridge of Trp27, Trp27 and Leu79, and now in the '''Closed Form'''. | ||
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Gln48 is crutial for some kind of actions of the entire Protein. ~Different colour, then link it to the Function Section. | |||
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The three loops 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 three loops 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. | ||
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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. | ||
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