PMID- 1055432
OWN - NLM
STAT- MEDLINE
DCOM- 19750804
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 72
IP  - 4
DP  - 1975 Apr
TI  - Evolutionary relationship between immunoglobulins and transplantation antigens.
PG  - 1612-6
AB  - The major human and murine histocompatibility antigens are tetrameric molecules
      with an apparent molecular weight of about 130,000. They are composed of two
      types of polypeptide chains. The two light chains, previously identified as
      beta2-microglobulins, are bound to the two heavy, alloantigenic HL-A or H-2
      polypeptide chains by noncovalent interactions only. The heavy chains are held
      together by disulfide bridge(s) located in the part of the molecule that is
      attached to the cell membrane. By limited proteolysis of the histocompatibility
      antigens evidence was obtained suggesting that the heavy chain may consist of
      three compact domains connected by more extended stretches of polypeptide chain. 
      Each domain appeared to contain a single disulfide bride encompassing about 60 to
      70 amino-acid residues. Staphylococcus aureus protein A is known to bind
      exclusively to the Fe region of immunoglobulin G. It was, however, observed that 
      protein A interacts in a similar way with the H-2 antigen heavy chain. This
      observation, together withthe homology of the primary structure of
      beta2-microglobulin to immunoglobulin G, the tetrameric structure of the
      alloantigens, the ogranizations of the heavy polypeptide chain into compact
      domains, and the presence of a single, immunoglobulin-like disulfide loop in each
      domain, establishes a close similarity in structure between histocompatibility
      antigens and immunoglobulins. The similarity in structural features suggests a
      common evolutionary origin of the two types of molecules.
FAU - Peterson, P A
AU  - Peterson PA
FAU - Rask, L
AU  - Rask L
FAU - Sege, K
AU  - Sege K
FAU - Klareskog, L
AU  - Klareskog L
FAU - Anundi, H
AU  - Anundi H
FAU - Ostberg, L
AU  - Ostberg L
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Disulfides)
RN  - 0 (HLA Antigens)
RN  - 0 (Histocompatibility Antigens)
RN  - 0 (Immunoglobulins)
RN  - 0 (Macromolecular Substances)
RN  - EC 3.4.22.2 (Papain)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - *Biological Evolution
MH  - Cell Membrane/immunology
MH  - Disulfides
MH  - HLA Antigens
MH  - *Histocompatibility Antigens
MH  - Humans
MH  - *Immunoglobulins
MH  - Macromolecular Substances
MH  - Mice
MH  - Molecular Weight
MH  - Papain
MH  - Protein Binding
MH  - Protein Conformation
MH  - Solubility
MH  - Spleen/immunology
PMC - PMC432589
EDAT- 1975/04/01 00:00
MHDA- 1975/04/01 00:01
CRDT- 1975/04/01 00:00
PHST- 1975/04/01 00:00 [pubmed]
PHST- 1975/04/01 00:01 [medline]
PHST- 1975/04/01 00:00 [entrez]
AID - 10.1073/pnas.72.4.1612 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1975 Apr;72(4):1612-6. doi: 10.1073/pnas.72.4.1612.