BIOMAT Database Logo BIOMAT Database Logo

Solution structure of human interleukin-1 receptor antagonist protein. 1994

B J Stockman, and T A Scahill, and N A Strakalaitis, and D P Brunner, and A W Yem, and M R Deibel
Upjohn Laboratories, Upjohn Company, Kalamazoo, MI 49007.

Interleukin-1 receptor antagonist protein (IRAP) is a naturally occurring inhibitor of the interleukin-1 receptor. In contrast to IL-1 beta, IRAP binds to the IL-1 receptor but does not elicit a physiological response. We have determined the solution structure of IRAP using NMR spectroscopy. While the overall topology of the two 153-residue proteins is quite similar, functionally critical differences exist concerning the residues of the linear amino acid sequence that constitute structurally homologous regions in the two proteins. Structurally homologous residues important for IL-1 receptor binding are conserved between IRAP and IL-1 beta. By contrast, structurally homologous residues critical for receptor activation are not conserved between the two proteins.

UI MeSH Term Description Entries
D007375 Interleukin-1 A soluble factor produced by MONOCYTES; MACROPHAGES, and other cells which activates T-lymphocytes and potentiates their response to mitogens or antigens. Interleukin-1 is a general term refers to either of the two distinct proteins, INTERLEUKIN-1ALPHA and INTERLEUKIN-1BETA. The biological effects of IL-1 include the ability to replace macrophage requirements for T-cell activation. IL-1,Lymphocyte-Activating Factor,Epidermal Cell Derived Thymocyte-Activating Factor,Interleukin I,Macrophage Cell Factor,T Helper Factor,Epidermal Cell Derived Thymocyte Activating Factor,Interleukin 1,Lymphocyte Activating Factor
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009682 Magnetic Resonance Spectroscopy Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING). In Vivo NMR Spectroscopy,MR Spectroscopy,Magnetic Resonance,NMR Spectroscopy,NMR Spectroscopy, In Vivo,Nuclear Magnetic Resonance,Spectroscopy, Magnetic Resonance,Spectroscopy, NMR,Spectroscopy, Nuclear Magnetic Resonance,Magnetic Resonance Spectroscopies,Magnetic Resonance, Nuclear,NMR Spectroscopies,Resonance Spectroscopy, Magnetic,Resonance, Magnetic,Resonance, Nuclear Magnetic,Spectroscopies, NMR,Spectroscopy, MR
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D012795 Sialoglycoproteins Glycoproteins which contain sialic acid as one of their carbohydrates. They are often found on or in the cell or tissue membranes and participate in a variety of biological activities. Polysialoglycoprotein,Sialoglycopeptide,Sialoglycopeptides,Sialoglycoprotein,Sialoprotein,Sialoproteins,Polysialoglycoproteins
D012996 Solutions The homogeneous mixtures formed by the mixing of a solid, liquid, or gaseous substance (solute) with a liquid (the solvent), from which the dissolved substances can be recovered by physical processes. (From Grant & Hackh's Chemical Dictionary, 5th ed) Solution
D017472 Receptors, Interleukin-1 Cell surface receptors that are specific for INTERLEUKIN-1. Included under this heading are signaling receptors, non-signaling receptors and accessory proteins required for receptor signaling. Signaling from interleukin-1 receptors occurs via interaction with SIGNAL TRANSDUCING ADAPTOR PROTEINS such as MYELOID DIFFERENTIATION FACTOR 88. IL-1 Receptor,IL-1 Receptors,IL1 Receptor,Interleukin-1 Receptor,Interleukin-1 Receptors,Receptor, Interleukin-1,Receptors, IL-1,IL1 Receptors,Interleukin 1 Receptor,IL 1 Receptor,IL 1 Receptors,Interleukin 1 Receptors,Receptor, IL-1,Receptor, IL1,Receptor, Interleukin 1,Receptors, IL 1,Receptors, IL1,Receptors, Interleukin 1

Related Publications

B J Stockman, and T A Scahill, and N A Strakalaitis, and D P Brunner, and A W Yem, and M R Deibel
Interleukin-1 receptor antagonist: discovery, structure and properties.
January 1990, Progress in growth factor research,
B J Stockman, and T A Scahill, and N A Strakalaitis, and D P Brunner, and A W Yem, and M R Deibel
Interleukin-1 receptor antagonist activity of a human interleukin-1 inhibitor.
January 1990, Nature,
B J Stockman, and T A Scahill, and N A Strakalaitis, and D P Brunner, and A W Yem, and M R Deibel
Initial crystallographic analysis of a recombinant human interleukin-1 receptor antagonist protein.
March 1994, Acta crystallographica. Section D, Biological crystallography,
B J Stockman, and T A Scahill, and N A Strakalaitis, and D P Brunner, and A W Yem, and M R Deibel
The mouse interleukin 1 receptor antagonist protein: gene structure and regulation in vitro.
January 1994, Cytokine,
B J Stockman, and T A Scahill, and N A Strakalaitis, and D P Brunner, and A W Yem, and M R Deibel
Interleukin-1 and interleukin-1 receptor antagonist.
January 1995, Nutrition (Burbank, Los Angeles County, Calif.),
B J Stockman, and T A Scahill, and N A Strakalaitis, and D P Brunner, and A W Yem, and M R Deibel
Interleukin-1 receptor antagonist.
January 1993, Advances in immunology,
B J Stockman, and T A Scahill, and N A Strakalaitis, and D P Brunner, and A W Yem, and M R Deibel
Interleukin-1 receptor antagonist.
August 1998, Rheumatic diseases clinics of North America,
B J Stockman, and T A Scahill, and N A Strakalaitis, and D P Brunner, and A W Yem, and M R Deibel
Interleukin-1 receptor antagonist.
January 1995, Critical reviews in immunology,
B J Stockman, and T A Scahill, and N A Strakalaitis, and D P Brunner, and A W Yem, and M R Deibel
Immunohistochemical demonstration of interleukin-1 receptor antagonist protein and interleukin-1 in human lymphoid tissue and granulomas.
February 1992, The American journal of pathology,
B J Stockman, and T A Scahill, and N A Strakalaitis, and D P Brunner, and A W Yem, and M R Deibel
Interleukin-1 receptor antagonist production by human keratinocytes.
January 1992, The Journal of investigative dermatology,
Copied contents to your clipboard!