1cwj: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (21 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL 3-S-METHYL-SARCOSINE CYCLOSPORIN== | ||
Eight new X-ray structures of different cyclophilin | <StructureSection load='1cwj' size='340' side='right'caption='[[1cwj]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1cwj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CWJ 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]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MSA:(2-S-METHYL)+SARCOSINE'>MSA</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</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=1cwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cwj OCA], [https://pdbe.org/1cwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cwj RCSB], [https://www.ebi.ac.uk/pdbsum/1cwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cwj ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | |||
== 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/cw/1cwj_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=1cwj ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Eight new X-ray structures of different cyclophilin A/cyclosporin-derivative complexes are presented. These structures, combined with the existing three published cyclosporin complexes, provide a useful structural database for the analysis of protein-ligand interactions. The effect of small chemical differences on protein-ligand hydrogen-bonding, van der Waals interactions and water structure is presented. | |||
X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A.,Kallen J, Mikol V, Taylor P, Walkinshaw MD J Mol Biol. 1998 Oct 23;283(2):435-49. PMID:9769216<ref>PMID:9769216</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1cwj" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Tolypocladium inflatum]] | ||
[[Category: Kallen | [[Category: Kallen J]] | ||
[[Category: Mikol | [[Category: Mikol V]] | ||
[[Category: Taylor | [[Category: Taylor P]] | ||
[[Category: Walkinshaw | [[Category: Walkinshaw MD]] | ||
Latest revision as of 08:54, 9 August 2023
HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL 3-S-METHYL-SARCOSINE CYCLOSPORINHUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL 3-S-METHYL-SARCOSINE CYCLOSPORIN
Structural highlights
FunctionPPIA_HUMAN PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedEight new X-ray structures of different cyclophilin A/cyclosporin-derivative complexes are presented. These structures, combined with the existing three published cyclosporin complexes, provide a useful structural database for the analysis of protein-ligand interactions. The effect of small chemical differences on protein-ligand hydrogen-bonding, van der Waals interactions and water structure is presented. X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A.,Kallen J, Mikol V, Taylor P, Walkinshaw MD J Mol Biol. 1998 Oct 23;283(2):435-49. PMID:9769216[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||||