title: Interaction between human interleukin-16 and CD4 receptor of HIV-1.
abstract: OBJECTIVE
  To study the interaction between human interleukin-16 (IL-16) and the receptor CD4 (T-lymphocyte differentiation antigen) of human immunodeficiency virus type 1 (HIV-1).
  
  
  METHODS
  Two structurally conserved regions (SCRs) of human IL-16 were built by the SYBYL/Biopolymer module using the corresponding transmembrane (TM) domain of human interleukin-4 (HIL-4) and HIL-2 as the templates. The coordinates for amino-terminal residue sequence, carboxyl-terminal residue sequences, and cytoplasm loops were generated using Biopolymer's LOOP SEARCH algorithm.
  
  
  RESULTS
  HIL-16 first formed a homodimer, then contacted with CD4 dimer further forming a dimeric complex. Subsequently, the dimeric complex constructed the tetrameric complex by two disulfide bridges between the cysteines of HIL-16 (Cys31-Cys31).
  
  
  CONCLUSIONS
  The interaction model is useful to propose the action mechanism of HIL-16 and is beneficial for rational designing of novel anti-HIV drugs.
authors.affiliation: Laboratory of Cellular and Molecule Evolution, Kunming Institute of Zoology, CAS, Kunming 650223, China.
authors.forename: J
authors.initials: J
authors.lastname: Yang
authors.forename: C Q
authors.initials: CQ
authors.lastname: Liu
mesh_terms: D000595:Amino Acid Sequence; D015704:CD4 Antigens / Q000737:chemistry* / Q000302:isolation & purification; D017076:Computer-Aided Design; D004347:Drug Interactions; D015497:HIV-1 / Q000276:immunology*; D006801:Humans; D019410:Interleukin-16 / Q000737:chemistry*; D007376:Interleukin-2 / Q000737:chemistry; D015847:Interleukin-4 / Q000737:chemistry; D011487:Protein Conformation; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013698:Templates, Genetic
chemical_list: D015704:CD4 Antigens; D019410:Interleukin-16; D007376:Interleukin-2; D015847:Interleukin-4