3H4Z

Crystal Structure of an MBP-Der p 7 fusion protein

Summary for 3H4Z

Entry DOI	10.2210/pdb3h4z/pdb
Related PRD ID	PRD_900001
Descriptor	Maltose-binding periplasmic protein fused with Allergen DERP7, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SODIUM ION, ... (4 entities in total)
Functional Keywords	mbp fusion, derp7, aha1/bpi domain-like, super roll, sugar transport, transport, allergen
Biological source	Escherichia coli More
Cellular location	Secreted: P49273
Total number of polymer chains	3
Total formula weight	188095.45
Authors	Pedersen, L.C.,Mueller, G.A.,London, R.E. (deposition date: 2009-04-21, release date: 2010-03-31, Last modification date: 2023-09-06)
Primary citation	Mueller, G.A.,Edwards, L.L.,Aloor, J.J.,Fessler, M.B.,Glesner, J.,Pomes, A.,Chapman, M.D.,London, R.E.,Pedersen, L.C. The structure of the dust mite allergen Der p 7 reveals similarities to innate immune proteins. J.Allergy Clin.Immunol., 125:909-917.e4, 2010 Cited by PubMed Abstract: Sensitization to house dust mite allergens is strongly correlated with asthma. Der p 7 elicits strong IgE antibody and T-cell responses in patients with mite allergy. However, the structure and biological function of this important allergen are unknown. Allergen function might contribute to allergenicity, as shown for the protease activity of group 1 mite allergens and the interaction with the innate immune system by group 2 mite allergens. PubMed: 20226507 DOI: 10.1016/j.jaci.2009.12.016 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.35 Å)

Structure validation