1yt2: Difference between revisions
New page: left|200px<br /><applet load="1yt2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yt2, resolution 3.25Å" /> '''Crystal Structure of... |
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[[Image:1yt2.gif|left|200px]]<br /><applet load="1yt2" size=" | [[Image:1yt2.gif|left|200px]]<br /><applet load="1yt2" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1yt2, resolution 3.25Å" /> | caption="1yt2, resolution 3.25Å" /> | ||
'''Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N APO CRYSTAL'''<br /> | '''Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N APO CRYSTAL'''<br /> | ||
==Overview== | ==Overview== | ||
GRP94, the endoplasmic reticulum paralog of Hsp90, is regulated by | GRP94, the endoplasmic reticulum paralog of Hsp90, is regulated by adenosine nucleotides that bind to its N-terminal regulatory domain. Because of its weak affinity for nucleotides, the functionally relevant transition in GRP94 is likely to be between the unliganded and nucleotide-bound states. We have determined the structure of the unliganded GRP94 N-domain. The helix 1-4-5 subdomain of the unliganded protein adopts the closed conformation seen in the structure of the protein in complex with inhibitors. This conformation is distinct from the open conformation of the subdomain seen when the protein is bound to ATP or ADP. ADP soaked into crystals of the unliganded protein reveals an intermediate conformation midway between the open and closed states and demonstrates that in GRP94 the conversion between the open and closed states is driven by ligand binding. The direction of the observed movement in GRP94 shows that nucleotides act to open the subdomain elements rather than close them, which is contrary to the motion proposed for Hsp90. These observations support a model where ATP binding dictates the conformation of the N-domain and regulates its ability to form quaternary structural interactions. | ||
==About this Structure== | ==About this Structure== | ||
1YT2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] with PG4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1YT2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] with <scene name='pdbligand=PG4:'>PG4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YT2 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Canis lupus familiaris]] | [[Category: Canis lupus familiaris]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dollins, D | [[Category: Dollins, D E.]] | ||
[[Category: Gewirth, D | [[Category: Gewirth, D T.]] | ||
[[Category: Immormino, R | [[Category: Immormino, R M.]] | ||
[[Category: PG4]] | [[Category: PG4]] | ||
[[Category: bergerat]] | [[Category: bergerat]] | ||
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[[Category: htpg]] | [[Category: htpg]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:47 2008'' | ||
Revision as of 17:08, 21 February 2008
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Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N APO CRYSTAL
OverviewOverview
GRP94, the endoplasmic reticulum paralog of Hsp90, is regulated by adenosine nucleotides that bind to its N-terminal regulatory domain. Because of its weak affinity for nucleotides, the functionally relevant transition in GRP94 is likely to be between the unliganded and nucleotide-bound states. We have determined the structure of the unliganded GRP94 N-domain. The helix 1-4-5 subdomain of the unliganded protein adopts the closed conformation seen in the structure of the protein in complex with inhibitors. This conformation is distinct from the open conformation of the subdomain seen when the protein is bound to ATP or ADP. ADP soaked into crystals of the unliganded protein reveals an intermediate conformation midway between the open and closed states and demonstrates that in GRP94 the conversion between the open and closed states is driven by ligand binding. The direction of the observed movement in GRP94 shows that nucleotides act to open the subdomain elements rather than close them, which is contrary to the motion proposed for Hsp90. These observations support a model where ATP binding dictates the conformation of the N-domain and regulates its ability to form quaternary structural interactions.
About this StructureAbout this Structure
1YT2 is a Single protein structure of sequence from Canis lupus familiaris with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change., Dollins DE, Immormino RM, Gewirth DT, J Biol Chem. 2005 Aug 26;280(34):30438-47. Epub 2005 Jun 11. PMID:15951571
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