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Related Concept Videos

Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Structural Protein Function01:56

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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Factors Affecting Illness01:18

Factors Affecting Illness

When a person's physical, emotional, intellectual, social development or spiritual functioning is compromised, this deviation from a healthy normal state is called illness. Illness creates stress that in turn harms individuals. Irritation, anger, denial, hopelessness, and fear are behavioral and emotional changes an individual experiences in the phases of illness. A variety of factors influence a person's health and well-being.
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Globular and Fibrous Proteins02:21

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Evaluating the Anti-depression Effect of Xiaoyaosan on Chronically-stressed Mice
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Structural and functional features of factor XI.

D Gailani1, S B Smith

  • 1Department of Pathology, Division of Hematology/Oncology, Vanderbilt University, Nashville, TN 37232-6307, USA. dave.gailani@vanderbilt.edu

Journal of Thrombosis and Haemostasis : JTH
|July 28, 2009
PubMed
Summary
This summary is machine-generated.

Factor XI (FXI), a unique coagulation protease, functions as a homodimer. Its structure facilitates binding to platelets and factor IX (FIX), crucial for blood clotting regulation.

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Area of Science:

  • Biochemistry
  • Hematology
  • Molecular Biology

Background:

  • Factor XI (FXI) is a distinct coagulation protease with unique structural and mechanistic properties.
  • FXI is a homodimer, comprising four apple domains and a protease domain per subunit.

Purpose of the Study:

  • To elucidate the structural and functional characteristics of Factor XI in coagulation.
  • To understand the activation mechanism and substrate interactions of FXI.

Main Methods:

  • Structural analysis of FXI's homodimeric and domain organization.
  • Investigation of FXI activation pathways involving cleavage and intermediate formation.
  • Characterization of binding interactions with platelets, high molecular weight kininogen, and factor IX (FIX).

Main Results:

  • FXI's apple domains form a disk-like structure enabling simultaneous binding to platelets and FIX.
  • Activation of FXI to FXIa involves cleavage at Arg369-Ile370, unmasking catalytic domains and FIX-binding exosites.
  • A 1/2-FXIa intermediate, with one activated subunit, efficiently activates FIX.

Conclusions:

  • The homodimeric structure of FXI is likely integral to its function in binding FIX and platelet surfaces.
  • FXI's unique structure and activation mechanism highlight its specific role in the coagulation cascade.
  • Understanding FXI's properties is key to exploring its therapeutic potential in hemostasis and thrombosis.