1qsd: Difference between revisions

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[[Image:1qsd.gif|left|200px]]<br /><applet load="1qsd" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1qsd.gif|left|200px]]<br /><applet load="1qsd" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1qsd, resolution 2.2Å" />

'''RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR'''<br />

==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 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.

==About this Structure==

1QSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1QSD OCA].

1QSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QSD OCA].

==Reference==

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[[Category: four-helix-bundle]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 00:56:~~34 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:18 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1qsd.gif|left|200px]]<br /><applet load="1qsd" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1qsd.gif|left|200px]]<br /><applet load="1qsd" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1qsd, resolution 2.2&Aring;" />
 '''RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR'''<br />
 ==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 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.
 ==About this Structure==
-QSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QSD OCA].
+QSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QSD OCA].
 ==Reference==
@@ Line 17: / Line 17: @@
 [[Category: four-helix-bundle]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:56:34 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:18 2008''