1l3p
From Proteopedia
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| - | [[Image:1l3p.jpg|left|200px]]<br /><applet load="1l3p" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1l3p, resolution 1.98Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF THE FUNCTIONAL DOMAIN OF THE MAJOR GRASS POLLEN ALLERGEN Phl p 5b'''<br /> | ||
| - | == | + | ==CRYSTAL STRUCTURE OF THE FUNCTIONAL DOMAIN OF THE MAJOR GRASS POLLEN ALLERGEN Phl p 5b== |
| + | <StructureSection load='1l3p' size='340' side='right'caption='[[1l3p]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1l3p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phleum_pratense Phleum pratense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L3P FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l3p OCA], [https://pdbe.org/1l3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l3p RCSB], [https://www.ebi.ac.uk/pdbsum/1l3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l3p ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MPA5B_PHLPR MPA5B_PHLPR] Has ribonuclease activity. May be involved in host-pathogen interactions. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l3/1l3p_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l3p ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The major allergen Phlp 5b from timothy grass pollen induces allergic rhinitis and bronchial asthma in millions of allergic patients worldwide. As an important step towards understanding the interactions between the pollen protein and components of the human immune system, the structure of the C-terminal key domain of Phlp 5b has been determined at 2.0 A resolution and refined to an R value of 19.7%. This is the first known allergen composed entirely of alpha-helices. The protein forms a dimer stabilized by one intermolecular disulfide bridge. Sequence homology suggests that at least all group V and group VI grass-pollen allergens belong to this new class of 'four-helix-bundle allergens'. | The major allergen Phlp 5b from timothy grass pollen induces allergic rhinitis and bronchial asthma in millions of allergic patients worldwide. As an important step towards understanding the interactions between the pollen protein and components of the human immune system, the structure of the C-terminal key domain of Phlp 5b has been determined at 2.0 A resolution and refined to an R value of 19.7%. This is the first known allergen composed entirely of alpha-helices. The protein forms a dimer stabilized by one intermolecular disulfide bridge. Sequence homology suggests that at least all group V and group VI grass-pollen allergens belong to this new class of 'four-helix-bundle allergens'. | ||
| - | + | Structure of the functional domain of the major grass-pollen allergen Phlp 5b.,Rajashankar K, Bufe A, Weber W, Eschenburg S, Lindner B, Betzel C Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1175-81. Epub 2002, Jun 20. PMID:12077438<ref>PMID:12077438</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1l3p" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Phleum pratense]] | [[Category: Phleum pratense]] | ||
| - | + | [[Category: Betzel C]] | |
| - | [[Category: Betzel | + | [[Category: Bufe A]] |
| - | [[Category: Bufe | + | [[Category: Eschenburg S]] |
| - | [[Category: Eschenburg | + | [[Category: Lindner B]] |
| - | [[Category: Lindner | + | [[Category: Rajashankar KR]] |
| - | [[Category: Rajashankar | + | [[Category: Weber W]] |
| - | [[Category: Weber | + | |
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Current revision
CRYSTAL STRUCTURE OF THE FUNCTIONAL DOMAIN OF THE MAJOR GRASS POLLEN ALLERGEN Phl p 5b
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