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[[Image:1jml.jpg|left|200px]]


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==Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design==
The line below this paragraph, containing "STRUCTURE_1jml", creates the "Structure Box" on the page.
<StructureSection load='1jml' size='340' side='right'caption='[[1jml]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_1jml| PDB=1jml  | SCENE= }}
<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>
 
</table>
'''Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design'''
== Function ==
 
[https://www.uniprot.org/uniprot/Q51912_FINMA Q51912_FINMA]
 
== Evolutionary Conservation ==
==Overview==
[[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/jm/1jml_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1jml ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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.


==About this Structure==
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>
1JML is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JML OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://www.ncbi.nlm.nih.gov/pubmed/11526208 11526208]
</div>
[[Category: Finegoldia magna]]
<div class="pdbe-citations 1jml" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: Baker, D.]]
<references/>
[[Category: Kim, D E.]]
__TOC__
[[Category: Kuhlman, B]]
</StructureSection>
[[Category: Neill, J W.O.]]
[[Category: Finegoldia magna ATCC 29328]]
[[Category: Zhang, K Y.J.]]
[[Category: Large Structures]]
[[Category: Carboxy-terminal beta-strand swapped.]]
[[Category: Baker D]]
[[Category: Domain swapped dimer]]
[[Category: Kim DE]]
[[Category: Four stranded beta-sheet with central alpha helix]]
[[Category: Kuhlman B]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:24:57 2008''
[[Category: O'Neill JW]]
[[Category: Zhang KYJ]]

Latest revision as of 08:42, 16 August 2023

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

1jml, resolution 1.90Å

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