1dkd: Difference between revisions

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[[Image:1dkd.~~gif~~|left|200px]]

[[Image:1dkd.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX~~'''~~

===CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX===

~~==Overview==~~

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The chaperonin GroEL is a double toriodal assembly that with its cochaperonin GroES facilitates protein folding with an ATP-dependent mechanism. Nonnative conformations of diverse protein substrates bind to the apical domains surrounding the opening of the double toroid's central cavity. Using phage display, we have selected peptides with high affinity for the isolated apical domain. We have determined the crystal structures of the complexes formed by the most strongly bound peptide with the isolated apical domain, ~~and with GroEL. The peptide interacts with~~ the ~~groove between paired alpha helices in a manner similar~~ to ~~that of~~ the ~~GroES mobile loop~~. ~~Our structural analysis~~, ~~combined with other results, suggests that various modes of molecular plasticity are responsible for tight promiscuous binding of nonnative substrates and their release into~~ the ~~shielded cis assembly~~.

The line below this paragraph, {{ABSTRACT_PUBMED_10619429}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10619429 is the PubMed ID number.

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==About this Structure==

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[[Category: Phage display]]

[[Category: Protein folding]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 13~~:57:00 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:12:03 2008''

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-[[Image:1dkd.gif|left|200px]]
+{{Seed}}
+[[Image:1dkd.png|left|200px]]
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 {{STRUCTURE_1dkd|  PDB=1dkd  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX'''
+===CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX===
-==Overview==
+<!--
-The chaperonin GroEL is a double toriodal assembly that with its cochaperonin GroES facilitates protein folding with an ATP-dependent mechanism. Nonnative conformations of diverse protein substrates bind to the apical domains surrounding the opening of the double toroid's central cavity. Using phage display, we have selected peptides with high affinity for the isolated apical domain. We have determined the crystal structures of the complexes formed by the most strongly bound peptide with the isolated apical domain, and with GroEL. The peptide interacts with the groove between paired alpha helices in a manner similar to that of the GroES mobile loop. Our structural analysis, combined with other results, suggests that various modes of molecular plasticity are responsible for tight promiscuous binding of nonnative substrates and their release into the shielded cis assembly.
+The line below this paragraph, {{ABSTRACT_PUBMED_10619429}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10619429 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10619429}}
 ==About this Structure==
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 [[Category: Phage display]]
 [[Category: Protein folding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:57:00 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:12:03 2008''