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PDBsum entry 1wu3
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Cytokine PDB id
1wu3

 

 

 

 

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Contents
Protein chain
161 a.a. *
Waters ×48
* Residue conservation analysis
PDB id:
1wu3
Name: Cytokine
Title: Crystal structure of recombinant murine interferon beta
Structure: Interferon beta. Chain: i. Synonym: ifn-beta. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.15Å     R-factor:   0.197     R-free:   0.247
Authors: T.Senda,S.Saitoh,Y.Mitsui
Key ref:
T.Senda et al. (1995). Refined crystal structure of recombinant murine interferon-beta at 2.15 A resolution. J Mol Biol, 253, 187-207. PubMed id: 7473712 DOI: 10.1006/jmbi.1995.0544
Date:
01-Dec-04     Release date:   14-Dec-04    
Supersedes: 1rmi
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01575  (IFNB_MOUSE) -  Interferon beta from Mus musculus
Seq:
Struc: 		182 a.a.
161 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1006/jmbi.1995.0544 J Mol Biol 253:187-207 (1995)
PubMed id: 7473712  
 
 
Refined crystal structure of recombinant murine interferon-beta at 2.15 A resolution.
T.Senda, S.Saitoh, Y.Mitsui.
 
  ABSTRACT  
 
The crystal structure of recombinant murine interferon-beta (reMuIFN-beta) has been refined at 2.15 A resolution using newly collected synchrotron data. Based on 11,228 reflections (8.0 to 2.15 A), a final R-factor of 19.1% (with a free R-factor of 25.8%) was obtained with a model obeying standard geometry within 0.013 A in bond lengths and 1.4 degrees in bond angles. Compared with the previously reported model, several amino acid residues in helix A are frame-shifted, the conformations are changed for parts of loops AB and BC, helix C is extended and a new short helix exists in loop CD. Evolutionary considerations taken together, the type I interferons appear to share common structural features with respect to the chain-folding topology and the hydrogen-bond networks between various polypeptide segments. Specifically, the disposition of the C-terminal segment of loop AB (after Arg33), known to be an important receptor-binding site, seems to be strictly maintained among the type I interferons. The exposed amino acid residues on helices A and C, which have recently been implicated as the binding site for another receptor molecule, are less well conserved. This may be responsible for varied cellular effects among the subtypes of type I interferons.
 
  Selected figure(s)  
 
Figure 5.
Figure 5. Hydrogen-bond networks between various segments. The broken lines represent hydrogen bonds, and the side-chains playing a key role in the networks are shown as thicker lines. Filled circles marked WAT represent bound water molecules. Hydrogen-bond networks are shown for the interface (a) between helix A and helix C, (b) that around Arg142 (helix E), (c) that between helix D and helix E and (d) that between loop AB and helix D. 		Figure 7.
Figure 7. Amino acid conservation rate as displayed on the three-dimensional crystal structure of MuIFN-b (the view direction is approximately the same as in Figure 3). (a) Front view with the hot area in top front. (b) Back view. Amino acid residues more than 80% conserved among the type I interferons are colored red, while those having a conservation ratio between 60 and 80% are colored yellow. The other, less conserved residues are colored white.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1995, 253, 187-207) copyright 1995.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18252254 Z.Li, J.J.Strunk, P.Lamken, J.Piehler, and T.Walz (2008).
The EM structure of a type I interferon-receptor complex reveals a novel mechanism for cytokine signaling.
  J Mol Biol, 377, 715-724.  
16734561 C.Sommereyns, and T.Michiels (2006).
N-glycosylation of murine IFN-beta in a putative receptor-binding region.
  J Interferon Cytokine Res, 26, 406-413.  
15032600 S.Pestka, C.D.Krause, D.Sarkar, M.R.Walter, Y.Shi, and P.B.Fisher (2004).
Interleukin-10 and related cytokines and receptors.
  Annu Rev Immunol, 22, 929-979.  
15546383 S.Pestka, C.D.Krause, and M.R.Walter (2004).
Interferons, interferon-like cytokines, and their receptors.
  Immunol Rev, 202, 8.  
10704203 L.Runkel, C.deDios, M.Karpusas, M.Betzenhauser, C.Muldowney, M.Zafari, C.D.Benjamin, S.Miller, P.S.Hochman, and A.Whitty (2000).
Systematic mutational mapping of sites on human interferon-beta-1a that are important for receptor binding and functional activity.
  Biochemistry, 39, 2538-2551.  
11169919 S.Pestka (2000).
The human interferon alpha species and receptors.
  Biopolymers, 55, 254-287.  
10971581 V.C.Blank, C.Peña, and L.P.Roguin (2000).
Suitable experimental conditions are required to characterize interferon-alpha2b synthetic peptides.
  Eur J Biochem, 267, 5711-5716.  
10547147 K.E.Mogensen, M.Lewerenz, J.Reboul, G.Lutfalla, and G.Uzé (1999).
The type I interferon receptor: structure, function, and evolution of a family business.
  J Interferon Cytokine Res, 19, 1069-1098.  
  10600026 S.L.Swann, F.W.Bazer, L.H.Villarete, A.Chung, and C.H.Pontzer (1999).
Functional characterization of monoclonal antibodies to interferon-tau.
  Hybridoma, 18, 399-405.  
9525899 L.Runkel, L.Pfeffer, M.Lewerenz, D.Monneron, C.H.Yang, A.Murti, S.Pellegrini, S.Goelz, G.Uzé, and K.Mogensen (1998).
Differences in activity between alpha and beta type I interferons explored by mutational analysis.
  J Biol Chem, 273, 8003-8008.  
9452365 A.P.Alexenko, D.W.Leaman, J.Li, and R.M.Roberts (1997).
The antiproliferative and antiviral activities of IFN-tau variants in human cells.
  J Interferon Cytokine Res, 17, 769-779.  
9342320 M.Karpusas, M.Nolte, C.B.Benton, W.Meier, W.N.Lipscomb, and S.Goelz (1997).
The crystal structure of human interferon beta at 2.2-A resolution.
  Proc Natl Acad Sci U S A, 94, 11813-11818.
PDB code: 1au1
  9144766 R.J.Simpson, A.Hammacher, D.K.Smith, J.M.Matthews, and L.D.Ward (1997).
Interleukin-6: structure-function relationships.
  Protein Sci, 6, 929-955.  
9197998 Y.Mitsui, and T.Senda (1997).
Elucidation of the basic three-dimensional structure of type I interferons and its functional and evolutionary implications.
  J Interferon Cytokine Res, 17, 319-326.  
8994971 R.Radhakrishnan, L.J.Walter, A.Hruza, P.Reichert, P.P.Trotta, T.L.Nagabhushan, and M.R.Walter (1996).
Zinc mediated dimer of human interferon-alpha 2b revealed by X-ray crystallography.
  Structure, 4, 1453-1463.
PDB code: 1rh2
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 code is shown on the right.

 

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