3NUL
Profilin I from Arabidopsis thaliana
Summary for 3NUL
| Entry DOI | 10.2210/pdb3nul/pdb |
| Descriptor | PROFILIN I, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | profilin, cytoskeleton, actin binding protein |
| Biological source | Arabidopsis thaliana (MOUSE EAR CRESS) |
| Cellular location | Cytoplasm, cytoskeleton (By similarity): Q42449 |
| Total number of polymer chains | 1 |
| Total formula weight | 14568.92 |
| Authors | Thorn, K.,Christensen, H.E.M.,Shigeta, R.,Huddler, D.,Chua, N.-H.,Shalaby, L.,Lindberg, U.,Schutt, C.E. (deposition date: 1996-11-27, release date: 1997-12-03, Last modification date: 2024-11-06) |
| Primary citation | Thorn, K.S.,Christensen, H.E.,Shigeta, R.,Huddler, D.,Shalaby, L.,Lindberg, U.,Chua, N.H.,Schutt, C.E. The crystal structure of a major allergen from plants. Structure, 5:19-32, 1997 Cited by PubMed Abstract: Profilins are small eukaryotic proteins involved in modulating the assembly of actin microfilaments in the cytoplasm. They are able to bind both phosphatidylinositol-4,5-bisphosphate and poly-L-proline (PLP) and thus play a critical role in signaling pathways. Plant profilins are of interest because immunological cross-reactivity between pollen and human profilin may be the cause of hay fever and broad allergies to pollens. PubMed: 9016723DOI: 10.1016/S0969-2126(97)00163-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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