3rvw

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==Crystal structure of Der p 1 complexed with Fab 4C1==
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#REDIRECT [[5vpg]] This PDB entry is obsolete and replaced by 5vpg
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<StructureSection load='3rvw' size='340' side='right' caption='[[3rvw]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3rvw]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Dermatophagoides_pteronyssinus Dermatophagoides pteronyssinus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RVW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RVW FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rvt|3rvt]], [[3rvu|3rvu]], [[3rvv|3rvv]], [[3rvx|3rvx]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_1_(mite) Peptidase 1 (mite)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.65 3.4.22.65] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rvw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rvw RCSB], [http://www.ebi.ac.uk/pdbsum/3rvw PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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House dust mites produce potent allergens, Der p 1 and Der f 1, that cause allergic sensitization and asthma. Der p 1 and Der f 1 are cysteine proteases that elicit IgE responses in 80% of mite-allergic subjects and have proinflammatory properties. Their antigenic structure is unknown. Here, we present crystal structures of natural Der p 1 and Der f 1 in complex with a monoclonal antibody, 4C1, which binds to a unique cross-reactive epitope on both allergens associated with IgE recognition. The 4C1 epitope is formed by almost identical amino acid sequences and contact residues. Mutations of the contact residues abrogate mAb 4C1 binding and reduce IgE antibody binding. These surface-exposed residues are molecular targets that can be exploited for development of recombinant allergen vaccines.
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Molecular determinants for antibody binding on group 1 house dust mite allergens.,Chruszcz M, Pomes A, Glesner J, Vailes LD, Osinski T, Porebski PJ, Majorek KA, Heymann PW, Platts-Mills TA, Minor W, Chapman MD J Biol Chem. 2012 Mar 2;287(10):7388-98. Epub 2011 Dec 30. PMID:22210776<ref>PMID:22210776</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Dermatophagoides pteronyssinus]]
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[[Category: Mus musculus]]
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[[Category: Chapman, M D.]]
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[[Category: Chruszcz, M.]]
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[[Category: Minor, W.]]
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[[Category: Pomes, A.]]
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[[Category: Vailes, L D.]]
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[[Category: Allergen-antibody complex]]
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[[Category: Hydrolase-immune system complex]]
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  1. REDIRECT 5vpg This PDB entry is obsolete and replaced by 5vpg

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