PMID- 10438516
OWN - NLM
STAT- MEDLINE
DCOM- 19990901
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 33
DP  - 1999 Aug 13
TI  - Identification of a CD4 domain required for interleukin-16 binding and lymphocyte
      activation.
PG  - 23387-95
AB  - Interleukin-16 (IL-16) activates CD4(+) cells, possibly by direct interaction
      with CD4. IL-16 structure and function are highly conserved across species,
      suggesting similar conservation of a putative IL-16 binding site on CD4.
      Comparison of the human CD4 amino acid sequence with that of several different
      species revealed that immunoglobulin-like domain 4 is the most conserved
      extracellular region. Potential interaction of this domain with IL-16 was studied
      by testing murine D4 sequence-based oligopeptides for inhibition of IL-16
      chemoattractant activity and inhibition of IL-16 binding to CD4 in vitro. Three
      contiguous 12-residue D4 region peptides (designated A, B, and C) blocked IL-16
      chemoattractant activity, with peptide B the most potent. Peptides A and B were
      synergistic for inhibition, but peptide C was not. Peptides A and B also blocked 
      IL-16 binding to CD4 in vitro, whereas peptide C did not. CD4, in addition to its
      known function as a receptor for major histocompatibility complex class II,
      contains a binding site for IL-16 in the D4 domain. The D4 residues required for 
      IL-16 binding overlap those previously shown to participate in CD4-CD4
      dimerization following class II major histocompatibility complex binding,
      providing a mechanistic explanation for the known function of IL-16 to inhibit
      the mixed lymphocyte reaction.
FAU - Liu, Y
AU  - Liu Y
AD  - Pulmonary Center, Boston University School of Medicine, Boston, Massachusetts
      02118, USA.
FAU - Cruikshank, W W
AU  - Cruikshank WW
FAU - O'Loughlin, T
AU  - O'Loughlin T
FAU - O'Reilly, P
AU  - O'Reilly P
FAU - Center, D M
AU  - Center DM
FAU - Kornfeld, H
AU  - Kornfeld H
LA  - eng
SI  - PDB/1CID
GR  - HL-32802/HL/NHLBI NIH HHS/United States
GR  - U19 AI41994/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (CD4 Antigens)
RN  - 0 (Interleukin-16)
RN  - 0 (Receptors, Interleukin-2)
RN  - 0 (Recombinant Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - CD4 Antigens/chemistry/*metabolism
MH  - Humans
MH  - Interleukin-16/antagonists & inhibitors/*metabolism
MH  - *Lymphocyte Activation
MH  - Male
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Receptors, Interleukin-2/antagonists & inhibitors
MH  - Recombinant Proteins/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Species Specificity
EDAT- 1999/08/07 00:00
MHDA- 1999/08/07 00:01
CRDT- 1999/08/07 00:00
PHST- 1999/08/07 00:00 [pubmed]
PHST- 1999/08/07 00:01 [medline]
PHST- 1999/08/07 00:00 [entrez]
AID - 10.1074/jbc.274.33.23387 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Aug 13;274(33):23387-95. doi: 10.1074/jbc.274.33.23387.