Chaperones: Difference between revisions

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== Structural highlights ==
== Structural highlights ==


Structurally, heat shock proteins have a N-terminal <scene name='59/591341/Nbd_hsp70/5'>ATPase domain</scene> followed by a <scene name='59/590651/Sbd_of_dnak/4'> substrate binding domain</scene> with elongated C-terminal. <scene name='59/591341/4jn4/2'>4JN4</scene> is a representative example of a chaperone system in complex with ADP.
Structurally, heat shock proteins have a N-terminal ATPase domain followed by a substrate binding domain with elongated C-terminal. These domains <scene name='59/591341/Transition1/2'>allosterically regulate</scene> the hsp70 functioning. <scene name='59/591341/4jn4/2'>4JN4</scene> is a representative example of a chaperone system in complex with ADP.
[[Image:1-s2.0-S0301462209000520-gr1.jpg|left|500px|thumb|Structural organization of Hsp70]]
[[Image:1-s2.0-S0301462209000520-gr1.jpg|left|500px|thumb|Structural organization of Hsp70]]
<scene name='59/591341/Binding/1'>TextToBeDisplayed</scene>
<scene name='59/591341/Binding/1'>TextToBeDisplayed</scene>


<scene name='59/591341/Transition1/2'>TextToBeDisplayed</scene>
</StructureSection>
</StructureSection>


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