3lka: Difference between revisions

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{{Seed}}
[[Image:3lka.jpg|left|200px]]


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==Catalytic domain of human MMP-12 complexed with hydroxamic acid and paramethoxy-sulfonyl amide==
The line below this paragraph, containing "STRUCTURE_3lka", creates the "Structure Box" on the page.
<StructureSection load='3lka' size='340' side='right'caption='[[3lka]], [[Resolution|resolution]] 1.80&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'>[[3lka]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LKA 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]] 1.8&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</scene>, <scene name='pdbligand=M4S:4-METHOXYBENZENESULFONAMIDE'>M4S</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_3lka|  PDB=3lka  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lka OCA], [https://pdbe.org/3lka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lka RCSB], [https://www.ebi.ac.uk/pdbsum/3lka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lka ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MMP12_HUMAN MMP12_HUMAN] May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.
== 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/lk/3lka_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=3lka ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
For several drug leads obtained by tethering weak binding ligands, the dissociation constant is smaller than the product of those of the individual fragments by a factor named the linking coefficient, E. This favorable contribution is attributed to the entropic gain that is realized when two weak binding ligands are tethered. Here we show a case study where the linking coefficient is strikingly small (E = 2.1 x 10(-3) M(-1)) and its totally entropic nature is demonstrated.


===Catalytic domain of human MMP-12 complexed with hydroxamic acid and paramethoxy-sulfonyl amide===
Entropic Contribution to the Linking Coefficient in Fragment Based Drug Design: A Case Study.,Borsi V, Calderone V, Fragai M, Luchinat C, Sarti N J Med Chem. 2010 Apr 23. PMID:20415416<ref>PMID:20415416</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3lka" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_20415416}}, adds the Publication Abstract to the page
*[[MHC 3D structures|MHC 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 20415416 is the PubMed ID number.
*[[MHC I 3D structures|MHC I 3D structures]]
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*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
{{ABSTRACT_PUBMED_20415416}}
== References ==
 
<references/>
==About this Structure==
__TOC__
3LKA is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LKA OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:20415416</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Macrophage elastase]]
[[Category: Large Structures]]
[[Category: Calderone, V.]]
[[Category: Calderone V]]
[[Category: Calcium]]
[[Category: Elastase]]
[[Category: Extracellular matrix]]
[[Category: Glycoprotein]]
[[Category: Hydrolase]]
[[Category: Matrix metalloproteinase]]
[[Category: Metal-binding]]
[[Category: Metallo elastase]]
[[Category: Metalloprotease]]
[[Category: Mmp12]]
 
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Retrieved from "https://proteopedia.org/3lka"