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Introduction

Protein: cHuman Coagulation factor V, 1czv ^[1]

spinqualitylabelsall models PDB ID 1czv Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1czv, resolution 2.40Å ()
Related:	1czs, 1czt
Structural annotation: Resources: CATH : 1Czva00, 1Czvb00 InterPro : Ipr008972, Ipr002355, Ipr011707, Ipr000421, Ipr008979, Ipr009271, Ipr014693 Pfam : PF00754 SCOP : d1czva_, d1czvb_ UniProt : P12259
Functional annotation: Cellular component: extracellular region Biological process: blood coagulation cell adhesion Molecular function: copper ion binding calcium ion binding metal ion binding oxidoreductase activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Contents 1 Introduction 1.1 Structure 1.2 Function 1.3 Interactions 2 References

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.
-Heavy A1-A2 Chain
-Light A3-C1-C2 Chain
FVa consists of a conserved β-Barrel framework acting as a scaffold for three loops and a C2 domain (FVa-C2).
The FVa-C2, which is classified as a distorted jelly-roll β-barrel motif, is compossed of eight major antiparallel strands arranged into two β-sheets of five and three strands packed against one another.
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..
The Three Loops
(1)-Ser21-Trp31
(2)-Asn39-Asn45
(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.

Which once activated, enhances the ability of factor Xa to generate α-thrombin from prothrombin (5-Fold).

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Function

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Interactions

References

1. ↑ 10586886