Related Experiment Videos

A new extra sequence at the amino terminal of a mu heavy chain disease protein (DAG)

C Mihaesco1, P Ferrara, J C Guillemot

  • 1Laboratoire d'Immunochimie et d'Immunopathologie, U.108 INSERM, Hôpital Saint-Louis, Paris, France.

Molecular Immunology
|August 1, 1990
PubMed

Insights

This study details the primary structure of the human mu heavy chain (DAG) protein, a circular decamer. Its unique N-terminal extra sequence shows no homology to known proteins.

Area of Science:

  • Immunology
  • Protein Chemistry
  • Molecular Biology

Background:

  • The human mu heavy chain (DAG) protein is a key component in immune responses.
  • Understanding its primary structure is crucial for elucidating its function and interactions.

Purpose of the Study:

  • To describe the primary structure of the human mu heavy chain (DAG) protein.
  • To characterize its oligomeric state, molecular weight, and constituent domains.
  • To identify and analyze the N-terminal extra sequence.

Main Methods:

  • Primary structure analysis of the human mu heavy chain (DAG) protein.
  • Determination of oligomeric state and molecular weight.
  • Sequence homology searches against protein databases.

Main Results:

  • The human mu heavy chain (DAG) protein exists as a circular decamer (500 kDa).
  • Each monomer comprises constant domains C mu 2, C mu 3, and C mu4, linked by 15 disulfide bridges.
  • An N-terminal extra sequence (Arg-Gln-Ser-Asp-Asp-Pro-Val-Leu-Arg-Gly-Thr-Thr-Val-Pro-Val-Thr-Glu) was identified, initiating at Val223.
  • This extra sequence exhibits no homology with existing protein databases.

Conclusions:

  • The human mu heavy chain (DAG) protein possesses a unique N-terminal sequence with no known homologs.
  • The described primary structure provides a foundation for further functional and structural studies of this protein.

Related Concept Videos