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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

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...

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Structural and functional characterization of human SLFN14.

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The Schlafen 14 (SLFN14) protein, crucial for immune and anti-tumor responses, possesses strong RNase activity but lacks helicase function. Its structure reveals key sites for oligonucleotide binding and potential multiple cellular conformations.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • The Schlafen (SLFN) protein family are DNA/RNA processing enzymes involved in immunological and anti-tumor processes.
  • SLFN14, a member of this family, exhibits antiviral activity and is linked to an inherited bleeding disorder.

Purpose of the Study:

  • To present the cryo-electron microscopy structure of full-length human SLFN14.
  • To elucidate the structural and biochemical features of SLFN14, including its enzymatic activities and potential cellular conformations.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) for structural determination.
  • Biochemical assays to assess RNase and helicase activity.
  • Live-cell fluorescence resonance energy transfer (FRET) assays and AlphaFold2 analysis for conformational studies.

Main Results:

  • The structure of full-length human SLFN14 was determined, revealing RNase, SWADL, and helicase domains.
  • SLFN14 demonstrated potent RNase activity, with specific charged patches in the RNase domain crucial for oligonucleotide binding.
  • SLFN14 lacked helicase activity due to an inability to bind ATP and the absence of positive charges in its DNA-binding site.
  • Structural comparisons showed SLFN14 is similar to SLFN11 but differs from SLFN5 in helicase domain orientation.
  • FRET assays and AlphaFold2 suggested SLFN14 may adopt multiple conformations in cells.

Conclusions:

  • Detailed structural and biochemical insights into SLFN14 were provided.
  • The findings expand the understanding of the functional diversity within the SLFN protein family.
  • The study highlights SLFN14's role in RNA processing and its potential implications in disease.