SMART: IL1 domain annotation

IL1 Interleukin-1 homologues

SMART accession number:	SM00125
Description:	Cytokines with various biological functions. Interluekin 1 alpha and beta are also known as hematopoietin and catabolin.
Family alignment:	View or

There are 2006 IL1 domains in 2001 proteins in SMART's nrdb database.

Click on the following links for more information.

Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing IL1 domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with IL1 domain is also avaliable.

Click on the protein counts, or double click on taxonomic names to display all proteins containing IL1 domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Dinarello CA
- Interleukin-1.
- Cytokine Growth Factor Rev. 1997; 8: 253-65
- Display abstract
- Interleukin-1 (IL-1) is the prototypic pro-inflammatory cytokine. There are two forms of IL-1, IL-1alpha and IL-1beta and in most studies, their biological activities are indistinguishable. IL-1 affects nearly every cell type, often in concert with another pro-inflammatory cytokine, tumor necrosis factor (TNF). Although IL-1 can upregulate host defenses and function as an immunoadjuvant, IL-1 is a highly inflammatory cytokine. The margin between clinical benefit and unacceptable toxicity in humans is exceedingly narrow. In contrast, agents that reduce the production and/or activity of IL-1 are likely to have an impact on clinical medicine. The synthesis, processing, secretion and activity of IL-1, particularly IL-1beta, are tightly regulated events. A unique aspect of cytokine biology is the naturally occurring IL-1 receptor antagonist (IL-1Ra). IL-1Ra is structurally similar to IL-1beta but lacking agonist activity is used in clinical trials to reduce disease severity. In addition, regulation of IL-1 activity extends to low numbers of surface receptors, circulating soluble receptors and a cell surface "decoy" receptor to down-regulate responses to IL-1beta. This review updates the current knowledge on IL-1.
- Patarca R, Fletcher MA
- Interleukin-1: basic science and clinical applications.
- Crit Rev Oncog. 1997; 8: 143-88
- Kurzrock R, Wetzler M, Estrov Z, Talpaz M
- Interleukin-1 and its inhibitors: a biologic and therapeutic model for the role of growth regulatory factors in leukemias.
- Cytokines Mol Ther. 1995; 1: 177-84
- Display abstract
- Production of growth factors may provide a mechanism for disease evolution in some leukemias. Interleukin-1 is a plelotropic cytokine with the ability to synergize with other growth factors as well as to stimulate their production and release. Autocrine and/or paracrine secretion of interleukin-1 has been implicated in the pathogenesis of both chronic and acute myelogenous leukemia. Recently, a series of both specific and nonspecific IL-1 inhibitory molecules have been identified. These include IL-1 receptor antagonist, soluble IL-1 receptors, IL-1-converting enzyme inhibitor, IL-4, IL-10 and IL-1-antisense. Early experiments demonstrating the ability of some of these molecules to inhibit acute and chronic myelogenous leukemia growth suggest that clinical trials of these compounds may provide a novel management approach in these malignancies. Here we review the potential biologic and therapeutic role of IL-1 and its inhibitors in the myeloid leukemias.
Metabolism (metabolic pathways involving proteins which contain this domain)

Structure (3D structures containing this domain)

3D Structures of IL1 domains in PDB

PDB code	Main view	Title
1hib		THE STRUCTURE OF AN INTERLEUKIN-1 BETA MUTANT WITH REDUCED BIOACTIVITY SHOWS MULTIPLE SUBTLE CHANGES IN CONFORMATION THAT AFFECT PROTEIN-PROTEIN RECOGNITION
1i1b		CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-1BETA AT 2.0 ANGSTROMS RESOLUTION
1ilr		CRYSTAL STRUCTURE OF THE INTERLEUKIN-1 RECEPTOR ANTAGONIST
1ilt		X-RAY STRUCTURE OF INTERLEUKIN-1 RECEPTOR ANTAGONIST AT 2.0 ANGSTROMS RESOLUTION
1iob		INTERLEUKIN-1 BETA FROM JOINT X-RAY AND NMR REFINEMENT
1ira		COMPLEX OF THE INTERLEUKIN-1 RECEPTOR WITH THE INTERLEUKIN-1 RECEPTOR ANTAGONIST (IL1RA)
1irp		SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN
1itb		TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA
1j0s		Solution structure of the human interleukin-18
1l2h		Crystal structure of Interleukin 1-beta F42W/W120F mutant
1md6		High resolution crystal structure of murine IL-1F5 reveals unique loop conformation for specificity
1s0l		Interleukin 1 beta mutant F42W
1t4q		Interleukin 1 beta F101W
1too		Interleukin 1B Mutant F146W
1tp0		Triple mutation in interleukin 1 beta cavity:replacement of phenylalanines with tryptophan.
1twe		INTERLEUKIN 1 BETA MUTANT F101Y
1twm		Interleukin-1 Beta Mutant F146Y
21bi		INTERLEUKIN-1 BETA (IL-1 BETA) (MUTANT WITH CYS 71 REPLACED BY ALA) (C71A)
2i1b		CRYSTALLOGRAPHIC REFINEMENT OF INTERLEUKIN-1 BETA AT 2.0 ANGSTROMS RESOLUTION
2ila		STRUCTURE OF INTERLEUKIN 1ALPHA AT 2.7-ANGSTROMS RESOLUTION
2irt		INITIAL CRYSTALLOGRAPHIC ANALYSES OF A RECOMBINANT INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN
2kh2		Solution structure of a scFv-IL-1B complex
2kki		Solution structure of human Interleukin 1a
2l5x		Solution structure of IL1A-S100A13 complex
2mib		THE STRUCTURE OF MURINE INTERLEUKIN-1 BETA AT 2.8 ANGSTROMS RESOLUTION
2nvh		Determination of Solvent Content in Cavities in Interleukin-1 Using Experimentally-Phased Electron Density
2vxt		Crystal structure of human IL-18 complexed to murine reference antibody 125-2H Fab
2wry		Crystal structure of chicken cytokine interleukin 1 beta
31bi		INTERLEUKIN-1 BETA (IL-1 BETA) (MUTANT WITH CYS 71 REPLACED BY SER) (C71S)
3f62		Crystal Structure of Human IL-18 in complex with Ectromelia virus IL-18 Binding Protein
3ltq		Structure of Interleukin 1B solved by SAD using an inserted Lanthanide Binding Tag
3nj5		Crystal structure of chicken IL-1 hydrophobic cavity mutant 157
3o4o		Crystal structure of an Interleukin-1 receptor complex
3pok		Interleukin-1-beta LBT L3 Mutant
3wo2		3WO2
3wo3		3WO3
3wo4		3WO4
41bi		INTERLEUKIN-1 BETA (IL-1 BETA) (MUTANT WITH CYS 8 REPLACED BY ALA (C8A)
4dep		Structure of the IL-1b signaling complex
4g6j		Crystal structure of human IL-1beta in complex with the therapeutic antibody binding fragment of canakinumab
4g6m		Crystal strucure of human IL-1beta in complex with therapeutic antibody binding fragment of gevokizumab
4gaf		Crystal structure of EBI-005, a chimera of human IL-1beta and IL-1Ra, bound to human Interleukin-1 receptor type 1
4gai		Crystal structure of EBI-005, a chimera of human IL-1beta and IL-1Ra
4hjj		Structure Reveals Function of the Dual Variable Domain Immunoglobulin (DVD-Ig) Molecule
4i1b		FUNCTIONAL IMPLICATIONS OF INTERLEUKIN-1BETA BASED ON THE THREE-DIMENSIONAL STRUCTURE
4ize		4IZE
4p0j		4P0J
4p0k		4P0K
4p0l		4P0L
4r6u		4R6U
4x37		4X37
4x38		4X38
4x39		4X39
4x3a		4X3A
4xfs		4XFS
5bow		5BOW
5bvp		5BVP
5i1b		A COMPARISON OF THE HIGH RESOLUTION STRUCTURES OF HUMAN AND MURINE INTERLEUKIN-1B
6i1b		HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN-1 BETA IN SOLUTION BY THREE-AND FOUR-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
7i1b		HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN-1 BETA IN SOLUTION BY THREE-AND FOUR-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
8i1b		A COMPARISON OF THE HIGH RESOLUTION STRUCTURES OF HUMAN AND MURINE INTERLEUKIN-1B
9ilb		HUMAN INTERLEUKIN-1 BETA

Links (links to other resources describing this domain)
PROSITE IL1_DOMAIN

IL1

Taxonomic distribution of proteins containing IL1 domain.

3D Structures of IL1 domains in PDB