1qsd: Difference between revisions

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-[[Image:1qsd.gif|left|200px]]
+{{Seed}}
+[[Image:1qsd.png|left|200px]]
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 {{STRUCTURE_1qsd|  PDB=1qsd  |  SCENE=  }}
-'''RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR'''
+===RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR===
-==Overview==
+<!--
-The folding pathway of tubulins includes highly specific interactions with a series of cofactors (A, B, C, D and E) after they are released from the eukaryotic chaperonin CCT. The 2.2 A crystal structure of Rbl2p, the Saccharomyces cerevisiae homolog of beta-tubulin specific cofactor A, shows alpha-helical monomers forming a flat, slightly convex dimer. The surface of the molecule is dominated by polar and charged residues and lacks hydrophobic patches typically observed for chaperones that bind unfolded or partially folded proteins. This post-chaperonin cofactor is therefore clearly distinct from typical chaperones where hydrophobicity is a hallmark of substrate recognition.
+The line below this paragraph, {{ABSTRACT_PUBMED_10542094}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10542094 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10542094}}
 ==About this Structure==
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 [[Category: Chaperone]]
 [[Category: Four-helix-bundle]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:39:03 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:28:46 2008''