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==Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ2==
==Crystal Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor FJ2==
<StructureSection load='4lwe' size='340' side='right' caption='[[4lwe]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='4lwe' size='340' side='right'caption='[[4lwe]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4lwe]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LWE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LWE FirstGlance]. <br>
<table><tr><td colspan='2'>[[4lwe]] 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=4LWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LWE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FJ2:N-[3-(5-CHLORO-2,4-DIHYDROXYPHENYL)-4-(4-METHOXYPHENYL)-1,2-OXAZOL-5-YL]ACETAMIDE'>FJ2</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lwf|4lwf]], [[4lwg|4lwg]], [[4lwh|4lwh]], [[4lwi|4lwi]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FJ2:N-[3-(5-CHLORO-2,4-DIHYDROXYPHENYL)-4-(4-METHOXYPHENYL)-1,2-OXAZOL-5-YL]ACETAMIDE'>FJ2</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lwe OCA], [http://pdbe.org/4lwe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lwe RCSB], [http://www.ebi.ac.uk/pdbsum/4lwe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lwe ProSAT]</span></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=4lwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lwe OCA], [https://pdbe.org/4lwe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lwe RCSB], [https://www.ebi.ac.uk/pdbsum/4lwe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lwe ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>
[https://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Heat Shock Proteins|Heat Shock Proteins]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: He, J]]
[[Category: Homo sapiens]]
[[Category: Li, J]]
[[Category: Large Structures]]
[[Category: Shi, F]]
[[Category: He J]]
[[Category: Xiong, B]]
[[Category: Li J]]
[[Category: Atp binding]]
[[Category: Shi F]]
[[Category: Chaperone]]
[[Category: Xiong B]]
[[Category: Molecularchaperone]]
[[Category: Rossmann fold]]

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