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Allergen PDB id
1q9b
Jmol
Contents
Protein chain
43 a.a. *
Ligands
MPD ×2
Waters ×39
* Residue conservation analysis
PDB id:
1q9b
Name: Allergen
Title: Crystal structure analysis of hev b 6.02 (hevein) at 1.5 angstroms resolution
Structure: Hevein. Chain: a. Synonym: hev b 6.02
Source: Hevea brasiliensis. Organism_taxid: 3981. Tissue: latex
Resolution:
1.50Å     R-factor:   0.128     R-free:   0.145
Authors: A.Rodriguez-Romero,A.Hernandez-Santoyo
Key ref: C.A.Reyes-López et al. (2004). Insights into a conformational epitope of Hev b 6.02 (hevein). Biochem Biophys Res Commun, 314, 123-130. PubMed id: 14715255 DOI: 10.1016/j.bbrc.2003.12.068
Date:
22-Aug-03     Release date:   13-Jan-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P02877  (HEVE_HEVBR) -  Pro-hevein
Seq:
Struc:
204 a.a.
43 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     cell wall macromolecule catabolic process   2 terms 
  Biochemical function     chitin binding     2 terms  

 

 
DOI no: 10.1016/j.bbrc.2003.12.068 Biochem Biophys Res Commun 314:123-130 (2004)
PubMed id: 14715255  
 
 
Insights into a conformational epitope of Hev b 6.02 (hevein).
C.A.Reyes-López, A.Hernández-Santoyo, M.Pedraza-Escalona, G.Mendoza, A.Hernández-Arana, A.Rodríguez-Romero.
 
  ABSTRACT  
 
Hevein (Hev b 6.02) is a major IgE-binding allergen in natural rubber latex and manufactured products. Both tryptophans (Trp(21) and Trp(23)) of the hevein molecule were chemically modified with BNPS-skatole (2-nitrophenylsulfenyl-3-methyl-3(')-bromoindolenine); derivatized allergen failed to significantly inhibit binding of serum IgE in ELISA assays. Similarly, skin prick tests showed that hevein-positive patients gave no response with the modified allergen. Dot blot experiments carried out with anti-hevein mono- and polyclonal antibodies confirmed the importance of Trp(21) and Trp(23) for antibody-recognition, and demonstrated the specific cross-reactivity of other molecules containing hevein-like domains. We also report the structure of Hev b 6.02 at an extended resolution (1.5A) and compare its surface properties around Trp residues with those of similar regions in other allergens. Overall our results indicate that the central part of the protein, which comprises three aromatic and other acidic and polar residues, constitutes a conformational epitope.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20652910 J.J.Hernández-Gay, A.Ardá, S.Eller, S.Mezzato, B.R.Leeflang, C.Unverzagt, F.J.Cañada, and J.Jiménez-Barbero (2010).
Insights into the dynamics and molecular recognition features of glycopeptides by protein receptors: the 3D solution structure of hevein bound to the trisaccharide core of N-glycoproteins.
  Chemistry, 16, 10715-10726.  
20544965 Y.Kezuka, M.Kojima, R.Mizuno, K.Suzuki, T.Watanabe, and T.Nonaka (2010).
Structure of full-length class I chitinase from rice revealed by X-ray crystallography and small-angle X-ray scattering.
  Proteins, 78, 2295-2305.
PDB code: 3iwr
18331637 K.Manikandan, D.Pal, S.Ramakumar, N.E.Brener, S.S.Iyengar, and G.Seetharaman (2008).
Functionally important segments in proteins dissected using Gene Ontology and geometric clustering of peptide fragments.
  Genome Biol, 9, R52.  
  17768356 D.Fuentes-Silva, G.Mendoza-Hernández, V.Stojanoff, L.A.Palomares, E.Zenteno, A.Torres-Larios, and A.Rodríguez-Romero (2007).
Crystallization and identification of the glycosylated moieties of two isoforms of the main allergen Hev b 2 and preliminary X-ray analysis of two polymorphs of isoform II.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 787-791.  
17724453 M.D.Cunningham (2007).
Neonatal latex allergy.
  J Perinatol, 27, 533-534.  
16264336 J.M.Rolland, A.C.Drew, and R.E.O'Hehir (2005).
Advances in development of hypoallergenic latex immunotherapy.
  Curr Opin Allergy Clin Immunol, 5, 544-551.  
16220560 M.I.Chávez, C.Andreu, P.Vidal, N.Aboitiz, F.Freire, P.Groves, J.L.Asensio, G.Asensio, M.Muraki, F.J.Cañada, and J.Jiménez-Barbero (2005).
On the importance of carbohydrate-aromatic interactions for the molecular recognition of oligosaccharides by proteins: NMR studies of the structure and binding affinity of AcAMP2-like peptides with non-natural naphthyl and fluoroaromatic residues.
  Chemistry, 11, 7060-7074.
PDB codes: 1znt 1zuv 1zwu
16335802 N.Kamal, S.Chowdhury, T.Madan, D.Sharma, M.Attreyi, W.Haq, S.B.Katti, A.Kumar, and P.U.Sarma (2005).
Tryptophan residue is essential for immunoreactivity of a diagnostically relevant peptide epitope of A. fumigatus.
  Mol Cell Biochem, 275, 223-231.  
15368576 N.Aboitiz, M.Vila-Perelló, P.Groves, J.L.Asensio, D.Andreu, F.J.Cañada, and J.Jiménez-Barbero (2004).
NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides.
  Chembiochem, 5, 1245-1255.
PDB code: 1t0w
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.