3lka

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:38, 6 September 2023) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3lka.png|left|200px]]
 
-
<!--
+
==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>
-
-->
+
<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>
-
The line below this paragraph, {{ABSTRACT_PUBMED_20415416}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 3lka" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 20415416 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_20415416}}
+
-
 
+
-
==About this Structure==
+
-
[[3lka]] is a 1 chain structure of [[Elastase]] 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].
+
==See Also==
==See Also==
-
*[[Elastase]]
+
*[[MHC 3D structures|MHC 3D structures]]
-
 
+
*[[MHC I 3D structures|MHC I 3D structures]]
-
==Reference==
+
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
-
<ref group="xtra">PMID:20415416</ref><references group="xtra"/>
+
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Macrophage elastase]]
+
[[Category: Large Structures]]
-
[[Category: Calderone, V.]]
+
[[Category: Calderone V]]
-
[[Category: Elastase]]
+
-
[[Category: Extracellular matrix]]
+
-
[[Category: Glycoprotein]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Matrix metalloproteinase]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: Metallo elastase]]
+
-
[[Category: Metalloprotease]]
+
-
[[Category: Mmp12]]
+

Current revision

Catalytic domain of human MMP-12 complexed with hydroxamic acid and paramethoxy-sulfonyl amide

PDB ID 3lka

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3lka"
Personal tools