3r91: Difference between revisions

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==Macrocyclic lactams as potent Hsp90 inhibitors with excellent tumor exposure and extended biomarker activity.==
==Macrocyclic lactams as potent Hsp90 inhibitors with excellent tumor exposure and extended biomarker activity.==
<StructureSection load='3r91' size='340' side='right' caption='[[3r91]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
<StructureSection load='3r91' size='340' side='right'caption='[[3r91]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3r91]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R91 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R91 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3r91]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R91 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=06H:(6S)-4,6,15,15,18-PENTAMETHYL-5,17-DIOXO-2,3,4,5,6,7,14,15,16,17-DECAHYDRO-1H-12,8-(METHENO)[1,4,9]TRIAZACYCLOTETRADECINO[9,8-A]INDOLE-9-CARBOXAMIDE'>06H</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=06H:(6S)-4,6,15,15,18-PENTAMETHYL-5,17-DIOXO-2,3,4,5,6,7,14,15,16,17-DECAHYDRO-1H-12,8-(METHENO)[1,4,9]TRIAZACYCLOTETRADECINO[9,8-A]INDOLE-9-CARBOXAMIDE'>06H</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90A, HSP90AA1, HSPC1, HSPCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90A, HSP90AA1, HSPC1, HSPCA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3r91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r91 OCA], [http://pdbe.org/3r91 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3r91 RCSB], [http://www.ebi.ac.uk/pdbsum/3r91 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3r91 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=3r91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r91 OCA], [https://pdbe.org/3r91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r91 RCSB], [https://www.ebi.ac.uk/pdbsum/3r91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r91 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/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Bloom, J D]]
[[Category: Bloom, J D]]
[[Category: Boschelli, F]]
[[Category: Boschelli, F]]
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