2JNZ
Solution structure of phl p 3, a major allergen from timothy grass pollen
Summary for 2JNZ
| Entry DOI | 10.2210/pdb2jnz/pdb |
| NMR Information | BMRB: 15134 |
| Descriptor | Phl p 3 allergen (1 entity in total) |
| Functional Keywords | allergen, timothy grass pollen |
| Biological source | Phleum pratense (timothy grass) |
| Total number of polymer chains | 1 |
| Total formula weight | 12248.87 |
| Authors | Schweimer, K.,Matecko, I.,Roesch, P. (deposition date: 2007-02-15, release date: 2008-03-04, Last modification date: 2023-12-20) |
| Primary citation | Schweimer, K.,Petersen, A.,Suck, R.,Becker, W.M.,Rosch, P.,Matecko, I. Solution structure of Phl p 3, a major allergen from timothy grass pollen Biol.Chem., 389:919-923, 2008 Cited by PubMed Abstract: The major 97-aa timothy grass (Phleum pratense) allergen Phl p 3 was recently isolated from an extract of timothy grass pollen. Sequence comparison classifies this protein as a group 3 allergen. The solution structure of Phl p 3 as determined by nuclear magnetic resonance spectroscopy reveals that the protein consists of a core of hydrophobic amino-acid side chains from two beta-sheets of five and four anti-parallel beta-strands, respectively. This conformation is very similar to the crystal structure published for Phl p 2 and strongly resembles the known conformation of the carboxy-terminal domain of Phl p 1, the major difference being the loop orientations. Phl p 2 and Phl p 3 show virtually identical immunoreactivity, and comparison of the charged surface amino acids of the two proteins gives initial clues as to the IgE recognition epitopes of these proteins. PubMed: 18627309DOI: 10.1515/BC.2008.102 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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