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3NUL

Profilin I from Arabidopsis thaliana

Summary for 3NUL
Entry DOI10.2210/pdb3nul/pdb
DescriptorPROFILIN I, SULFATE ION, GLYCEROL, ... (4 entities in total)
Functional Keywordsprofilin, cytoskeleton, actin binding protein
Biological sourceArabidopsis thaliana (MOUSE EAR CRESS)
Cellular locationCytoplasm, cytoskeleton (By similarity): Q42449
Total number of polymer chains1
Total formula weight14568.92
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 citationThorn, 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: 9016723
DOI: 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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