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New page: left|200px<br /><applet load="1hle" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hle, resolution 1.95Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1hle.jpg|left|200px]]<br /><applet load="1hle" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hle, resolution 1.95&Aring;" />
'''CRYSTAL STRUCTURE OF CLEAVED EQUINE LEUCOCYTE ELASTASE INHIBITOR DETERMINED AT 1.95 ANGSTROMS RESOLUTION'''<br />


==Overview==
==CRYSTAL STRUCTURE OF CLEAVED EQUINE LEUCOCYTE ELASTASE INHIBITOR DETERMINED AT 1.95 ANGSTROMS RESOLUTION==
The crystal structure of active-site cleaved equine leucocyte elastase, inhibitor, a member of the serpin superfamily, has been solved and refined, to a crystallographic R-factor of 17.6% at 1.95 A resolution. Despite, being an intracellular inhibitor with rather low sequence homology of 30%, to human alpha 1-antichymotrypsin and alpha 1-proteinase inhibitor, the, three-dimensional structures are very similar, with deviations only at the, sites of insertions and few mobile secondary structure elements. The, better resolution in comparison with the structures of other cleaved, serpins allows a more precise description of the so-called R-state of the, serpins.
<StructureSection load='1hle' size='340' side='right'caption='[[1hle]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hle]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HLE 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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1hle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hle OCA], [https://pdbe.org/1hle PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hle RCSB], [https://www.ebi.ac.uk/pdbsum/1hle PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hle ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ILEU_HORSE ILEU_HORSE] Thought to be involved in the control of intracellular protein turnover.
== 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/hl/1hle_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=1hle ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1HLE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with CA and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HLE OCA].
*[[Serpin 3D structures|Serpin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution., Baumann U, Bode W, Huber R, Travis J, Potempa J, J Mol Biol. 1992 Aug 20;226(4):1207-18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1518052 1518052]
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Baumann, U.]]
[[Category: Baumann U]]
[[Category: Bode, W.]]
[[Category: Bode W]]
[[Category: Huber, R.]]
[[Category: Huber R]]
[[Category: Potempa, J.]]
[[Category: Potempa J]]
[[Category: Travis, J.]]
[[Category: Travis J]]
[[Category: ACE]]
[[Category: CA]]
[[Category: hydrolase inhibitor(serine proteinase)]]
 
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