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Cytokine PDB id
2ila
Jmol
Contents
Protein chain
145 a.a.* *
* Residue conservation analysis
* C-alpha coords only
PDB id:
2ila
Name: Cytokine
Title: Structure of interleukin 1alpha at 2.7-angstroms resolution
Structure: Interleukin-1 alpha. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.30Å     R-factor:   0.190    
Authors: B.J.Graves,M.H.Hatada
Key ref:
B.J.Graves et al. (1990). Structure of interleukin 1 alpha at 2.7-A resolution. Biochemistry, 29, 2679-2684. PubMed id: 2346741 DOI: 10.1021/bi00463a009
Date:
01-May-91     Release date:   15-Oct-92    
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01583  (IL1A_HUMAN) -  Interleukin-1 alpha
Seq:
Struc: 		271 a.a.
145 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   2 terms 
  Biological process     immune response   2 terms 
  Biochemical function     interleukin-1 receptor binding     1 term  

 

 
    Key reference    
 
 
DOI no: 10.1021/bi00463a009 Biochemistry 29:2679-2684 (1990)
PubMed id: 2346741  
 
 
Structure of interleukin 1 alpha at 2.7-A resolution.
B.J.Graves, M.H.Hatada, W.A.Hendrickson, J.K.Miller, V.S.Madison, Y.Satow.
 
  ABSTRACT  
 
The interleukin 1 (IL-1) family of proteins has a central role in modulating immune and inflammatory responses. Two major IL-1 proteins, designated alpha (IL-1 alpha) and beta (IL-1 beta), are produced by activated macrophages and other cell types. In an effort to understand the similarities and differences in the physicochemical and functional properties of these two proteins, a program was initiated to determine their structures. Crystals of IL-1 alpha were grown, and the three-dimensional structure at 2.7-A resolution was solved. The technique of multiple-wavelength anomalous dispersion (MAD) with the selenomethionine form of IL-1 alpha was utilized in combination with a single mercury derivative to provide the starting phases. Partial refinement of the IL-1 alpha model has been performed as well. The overall structure is composed of 14 beta-strands and a 3(10) helix. The core of this structure is a capped beta-barrell that possesses 3-fold symmetry and displays a topology similar to and soybean trypsin inhibitor (STI) [McLachlan, A. D. (1979) J. Mol. Biol. 133, 557-563]. In this paper, the overall structure of IL-1 alpha and the nature and fidelity of the internal 3-fold symmetry are discussed. Comparisons with IL-1 beta and STI are made within these contexts.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20177398 C.Gabay, C.Lamacchia, and G.Palmer (2010).
IL-1 pathways in inflammation and human diseases.
  Nat Rev Rheumatol, 6, 232-241.  
19846555 M.Renko, J.Sabotic, M.Mihelic, J.Brzin, J.Kos, and D.Turk (2010).
Versatile loops in mycocypins inhibit three protease families.
  J Biol Chem, 285, 308-316.
PDB codes: 3h6q 3h6r 3h6s
19836339 A.Lingel, T.M.Weiss, M.Niebuhr, B.Pan, B.A.Appleton, C.Wiesmann, J.F.Bazan, and W.J.Fairbrother (2009).
Structure of IL-33 and its interaction with the ST2 and IL-1RAcP receptors--insight into heterotrimeric IL-1 signaling complexes.
  Structure, 17, 1398-1410.
PDB code: 2kll
17786931 I.Prudovsky, F.Tarantini, M.Landriscina, D.Neivandt, R.Soldi, A.Kirov, D.Small, K.M.Kathir, D.Rajalingam, and T.K.Kumar (2008).
Secretion without Golgi.
  J Cell Biochem, 103, 1327-1343.  
18320584 M.Li, Y.Huang, and Y.Xiao (2008).
Effects of external interactions on protein sequence-structure relations of beta-trefoil fold.
  Proteins, 72, 1161-1170.  
17340198 G.Vergoten, and J.P.Zanetta (2007).
Structural differences between the putative carbohydrate-recognition domains of human IL-1 alpha, IL-1 beta and IL-1 receptor antagonist obtained by in silico modeling.
  Glycoconj J, 24, 183-193.  
15297877 R.A.Kovall, and W.A.Hendrickson (2004).
Crystal structure of the nuclear effector of Notch signaling, CSL, bound to DNA.
  EMBO J, 23, 3441-3451.
PDB code: 1ttu
12794857 N.Lozovaya, and A.D.Miller (2003).
Chemical neuroimmunology: health in a nutshell bidirectional communication between immune and stress (limbic-hypothalamic-pituitary-adrenal) systems.
  Chembiochem, 4, 466-484.  
11948621 N.Kureishy, V.Sapountzi, S.Prag, N.Anilkumar, and J.C.Adams (2002).
Fascins, and their roles in cell structure and function.
  Bioessays, 24, 350-361.  
11714927 S.R.Brych, S.I.Blaber, T.M.Logan, and M.Blaber (2001).
Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a beta-trefoil.
  Protein Sci, 10, 2587-2599.
PDB codes: 1jqz 1jt3 1jt4 1jt5 1jt7 1jtc
10748229 Y.Liu, A.J.Chirino, Z.Misulovin, C.Leteux, T.Feizi, M.C.Nussenzweig, and P.J.Bjorkman (2000).
Crystal structure of the cysteine-rich domain of mannose receptor complexed with a sulfated carbohydrate ligand.
  J Exp Med, 191, 1105-1116.
PDB codes: 1dqg 1dqo
10328267 J.K.Dattagupta, A.Podder, C.Chakrabarti, U.Sen, D.Mukhopadhyay, S.K.Dutta, and M.Singh (1999).
Refined crystal structure (2.3 A) of a double-headed winged bean alpha-chymotrypsin inhibitor and location of its second reactive site.
  Proteins, 35, 321-331.
PDB code: 2wbc
10531477 S.Ravichandran, U.Sen, C.Chakrabarti, and J.K.Dattagupta (1999).
Cryocrystallography of a Kunitz-type serine protease inhibitor: the 90 K structure of winged bean chymotrypsin inhibitor (WCI) at 2.13 A resolution.
  Acta Crystallogr D Biol Crystallogr, 55, 1814-1821.
PDB code: 4wbc
  9646173 C.A.Dinarello (1998).
Interleukin-1, interleukin-1 receptors and interleukin-1 receptor antagonist.
  Int Rev Immunol, 16, 457-499.  
  10082365 T.D.Osslund, R.Syed, E.Singer, E.W.Hsu, R.Nybo, B.L.Chen, T.Harvey, T.Arakawa, L.O.Narhi, A.Chirino, and C.F.Morris (1998).
Correlation between the 1.6 A crystal structure and mutational analysis of keratinocyte growth factor.
  Protein Sci, 7, 1681-1690.  
8968609 B.S.Chang, R.M.Beauvais, T.Arakawa, L.O.Narhi, A.Dong, D.I.Aparisio, and J.F.Carpenter (1996).
Formation of an active dimer during storage of interleukin-1 receptor antagonist in aqueous solution.
  Biophys J, 71, 3399-3406.  
7601089 A.R.Bernard, T.N.Wells, A.Cleasby, F.Borlat, M.A.Payton, and A.E.Proudfoot (1995).
Selenomethionine labelling of phosphomannose isomerase changes its kinetic properties.
  Eur J Biochem, 230, 111-118.  
7499217 C.Guo, S.K.Dower, D.Holowka, and B.Baird (1995).
Fluorescence resonance energy transfer reveals interleukin (IL)-1-dependent aggregation of IL-1 type I receptors that correlates with receptor activation.
  J Biol Chem, 270, 27562-27568.  
7665610 H.Zhu, K.Ramnarayan, J.Anchin, W.Y.Miao, A.Sereno, L.Millman, J.Zheng, V.N.Balaji, and M.E.Wolff (1995).
Glu-96 of basic fibroblast growth factor is essential for high affinity receptor binding. Identification by structure-based site-directed mutagenesis.
  J Biol Chem, 270, 21869-21874.  
7673234 S.A.Greenfeder, T.Varnell, G.Powers, K.Lombard-Gillooly, D.Shuster, K.W.McIntyre, D.E.Ryan, W.Levin, V.Madison, and G.Ju (1995).
Insertion of a structural domain of interleukin (IL)-1 beta confers agonist activity to the IL-1 receptor antagonist. Implications for IL-1 bioactivity.
  J Biol Chem, 270, 22460-22466.  
  7579653 S.R.Price, and K.Nagai (1995).
Protein engineering as a tool for crystallography.
  Curr Opin Biotechnol, 6, 425-430.  
  7691311 A.E.Eriksson, L.S.Cousens, and B.W.Matthews (1993).
Refinement of the structure of human basic fibroblast growth factor at 1.6 A resolution and analysis of presumed heparin binding sites by selenate substitution.
  Protein Sci, 2, 1274-1284.
PDB codes: 1fga 4fgf
8436121 A.Hädener, P.K.Matzinger, V.N.Malashkevich, G.V.Louie, S.P.Wood, P.Oliver, P.R.Alefounder, A.R.Pitt, C.Abell, and A.R.Battersby (1993).
Purification, characterization, crystallisation and X-ray analysis of selenomethionine-labelled hydroxymethylbilane synthase from Escherichia coli.
  Eur J Biochem, 211, 615-624.  
8436117 F.Guinet, J.D.Guitton, N.Gault, F.Folliard, N.Touchet, J.M.Cherel, A.Crespo, A.Destourbe, P.Bertrand, and P.Denefle (1993).
Interleukin-1 beta-specific partial agonists defined by site-directed mutagenesis studies.
  Eur J Biochem, 211, 583-590.  
  8415875 Y.Mitsui, T.Senda, T.Shimazu, S.Matsuda, and J.Utsumi (1993).
Structural, functional and evolutionary implications of the three-dimensional crystal structure of murine interferon-beta.
  Pharmacol Ther, 58, 93.  
1553379 B.Veerapandian, G.L.Gilliland, R.Raag, A.L.Svensson, Y.Masui, Y.Hirai, and T.L.Poulos (1992).
Functional implications of interleukin-1 beta based on the three-dimensional structure.
  Proteins, 12, 10-23.
PDB code: 4i1b
1534698 B.Veerapandian (1992).
Structure and function of interleukin-1, based on crystallographic and modeling studies.
  Biophys J, 62, 112-115.
PDB codes: 1ita 1itn
1553380 E.A.Stura, P.Chen, C.M.Wilmot, J.H.Arevalo, and I.A.Wilson (1992).
Crystallization studies of glycosylated and unglycosylated human recombinant interleukin-2.
  Proteins, 12, 24-30.  
1528078 M.D.Walkinshaw (1992).
Protein targets for structure-based drug design.
  Med Res Rev, 12, 317-372.  
1388674 P.Manavalan, D.L.Swope, and R.M.Withy (1992).
Sequence and structural relationships in the cytokine family.
  J Protein Chem, 11, 321-331.  
  1369391 P.R.Young (1992).
Protein hormones and their receptors.
  Curr Opin Biotechnol, 3, 408-421.  
1555590 V.Carinci, S.Guida, M.R.Fontana, E.Palla, M.Rossini, and M.Melli (1992).
Processing of interleukin-1 in cells of monocytic lineage is differentiation-dependent.
  Eur J Biochem, 205, 295-301.  
1707542 A.E.Eriksson, L.S.Cousens, L.H.Weaver, and B.W.Matthews (1991).
Three-dimensional structure of human basic fibroblast growth factor.
  Proc Natl Acad Sci U S A, 88, 3441-3445.  
1781888 C.S.Wu, S.A.Thompson, and J.T.Yang (1991).
Basic fibroblast growth factor is a beta-rich protein.
  J Protein Chem, 10, 427-436.  
1837145 E.Labriola-Tompkins, C.Chandran, K.L.Kaffka, D.Biondi, B.J.Graves, M.Hatada, V.S.Madison, J.Karas, P.L.Kilian, and G.Ju (1991).
Identification of the discontinuous binding site in human interleukin 1 beta for the type I interleukin 1 receptor.
  Proc Natl Acad Sci U S A, 88, 11182-11186.  
1828896 S.P.Eisenberg, M.T.Brewer, E.Verderber, P.Heimdal, B.J.Brandhuber, and R.C.Thompson (1991).
Interleukin 1 receptor antagonist is a member of the interleukin 1 gene family: evolution of a cytokine control mechanism.
  Proc Natl Acad Sci U S A, 88, 5232-5236.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.