1BMW
A fibronectin type III fold in plant allergens: The solution structure of Phl PII from timothy grass pollen, NMR, 38 STRUCTURES
Summary for 1BMW
Entry DOI | 10.2210/pdb1bmw/pdb |
Descriptor | POLLEN ALLERGEN PHL P2 (1 entity in total) |
Functional Keywords | allergen, allergy, immunoglobulins, immunology |
Biological source | Phleum pratense (timothy grass) |
Total number of polymer chains | 1 |
Total formula weight | 10828.06 |
Authors | De Marino, S.,Morelli, M.A.C.,Fraternali, F.,Tamborino, E.,Vrtala, S.,Dolecek, C.,Arosio, P.,Valenta, R.,Pastore, A. (deposition date: 1998-07-27, release date: 1999-01-13, Last modification date: 2024-05-22) |
Primary citation | De Marino, S.,Morelli, M.A.,Fraternali, F.,Tamborino, E.,Vrtala, S.,Dolocek, C.,Arosio, P.,Valenta, R.,Pastore, A. An Immunoglobulin-Like Fold in a Major Plant Allergen: The Solution Structure of Phl P 2 from Timothy Grass Pollen. Structure Fold.Des., 7:943-952, 1999 Cited by PubMed Abstract: Grass pollen allergens are the most important and widespread elicitors of pollen allergy. One of the major plant allergens which millions of people worldwide are sensitized to is Phl p 2, a small protein from timothy grass pollen. Phl p 2 is representative of the large family of cross-reacting plant allergens classified as group 2/3. Recombinant Phl p 2 has been demonstrated by immunological cross-reactivity studies to be immunologically equivalent to the natural protein. PubMed: 10467147DOI: 10.1016/S0969-2126(99)80121-X PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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