1jml

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(New page: 200px<br /><applet load="1jml" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jml, resolution 1.90&Aring;" /> '''Conversion of Monome...)
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[[Image:1jml.jpg|left|200px]]<br /><applet load="1jml" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jml, resolution 1.90&Aring;" />
 
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'''Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design'''<br />
 
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==Overview==
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==Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design==
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Protein L consists of a single alpha-helix packed on a four-stranded, beta-sheet formed by two symmetrically opposed beta-hairpins. We use a, computer-based protein design procedure to stabilize a domain-swapped, dimer of protein L in which the second beta-turn straightens and the, C-terminal strand inserts into the beta-sheet of the partner. The designed, obligate dimer contains three mutations (A52V, N53P, and G55A) and has a, dissociation constant of approximately 700 pM, which is comparable to the, dissociation constant of many naturally occurring protein dimers. The, structure of the dimer has been determined by x-ray crystallography and is, close to the in silico model.
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<StructureSection load='1jml' size='340' side='right'caption='[[1jml]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1jml]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Finegoldia_magna_ATCC_29328 Finegoldia magna ATCC 29328]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JML FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jml OCA], [https://pdbe.org/1jml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jml RCSB], [https://www.ebi.ac.uk/pdbsum/1jml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jml ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q51912_FINMA Q51912_FINMA]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jm/1jml_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1jml ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protein L consists of a single alpha-helix packed on a four-stranded beta-sheet formed by two symmetrically opposed beta-hairpins. We use a computer-based protein design procedure to stabilize a domain-swapped dimer of protein L in which the second beta-turn straightens and the C-terminal strand inserts into the beta-sheet of the partner. The designed obligate dimer contains three mutations (A52V, N53P, and G55A) and has a dissociation constant of approximately 700 pM, which is comparable to the dissociation constant of many naturally occurring protein dimers. The structure of the dimer has been determined by x-ray crystallography and is close to the in silico model.
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==About this Structure==
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Conversion of monomeric protein L to an obligate dimer by computational protein design.,Kuhlman B, O'Neill JW, Kim DE, Zhang KY, Baker D Proc Natl Acad Sci U S A. 2001 Sep 11;98(19):10687-91. Epub 2001 Aug 28. PMID:11526208<ref>PMID:11526208</ref>
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1JML is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JML OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Conversion of monomeric protein L to an obligate dimer by computational protein design., Kuhlman B, O'Neill JW, Kim DE, Zhang KY, Baker D, Proc Natl Acad Sci U S A. 2001 Sep 11;98(19):10687-91. Epub 2001 Aug 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11526208 11526208]
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</div>
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[[Category: Finegoldia magna]]
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<div class="pdbe-citations 1jml" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Baker, D.]]
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<references/>
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[[Category: Kim, D.E.]]
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__TOC__
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[[Category: Kuhlman, B]]
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</StructureSection>
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[[Category: Neill, J.W.O.]]
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[[Category: Finegoldia magna ATCC 29328]]
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[[Category: Zhang, K.Y.J.]]
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[[Category: Large Structures]]
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[[Category: ZN]]
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[[Category: Baker D]]
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[[Category: carboxy-terminal beta-strand swapped.]]
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[[Category: Kim DE]]
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[[Category: domain swapped dimer]]
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[[Category: Kuhlman B]]
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[[Category: four stranded beta-sheet with central alpha helix]]
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[[Category: O'Neill JW]]
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[[Category: Zhang KYJ]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:52:50 2007''
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Current revision

Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design

PDB ID 1jml

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