1itl
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HUMAN INTERLEUKIN 4: THE SOLUTION STRUCTURE OF A FOUR-HELIX-BUNDLE PROTEIN
OverviewOverview
Heteronuclear 13C and 15N three-dimensional nuclear magnetic resonance, (n.m.r.) techniques have been used to determine the solution structure of, human interleukin 4, a four-helix bundle protein. A dynamical simulated, annealing protocol was used to calculate an ensemble of structures from an, n.m.r. data set of 1735 distance restraints, 101 phi angle restraints and, 27 pairs of hydrogen bond restraints. The protein structure has a, left-handed up-up-down-down topology for the four helices with the two, long overhand loops in the structure being connected by a short section of, irregular antiparallel beta-sheet. Analysis of the side-chains in the, protein shows a clustering of hydrophobic residues, particularly leucines, in the core of the bundle with the side-chains of charged residues being, located on the protein surface. The solution structure has been compared, with a recent structure prediction for human interleukin 4 and with, crystal structures of other helix bundle proteins.
DiseaseDisease
Known diseases associated with this structure: AIDS, slow progression to OMIM:[147781], Atopy, susceptibility to OMIM:[147781]
About this StructureAbout this Structure
1ITL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Human interleukin 4. The solution structure of a four-helix bundle protein., Smith LJ, Redfield C, Boyd J, Lawrence GM, Edwards RG, Smith RA, Dobson CM, J Mol Biol. 1992 Apr 20;224(4):899-904. PMID:1569578
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