1gml: Difference between revisions

Line 4:

==Overview==

The chaperonin containing TCP-1 (CCT, also known as TRiC) is the only, member of the chaperonin family found in the cytosol of eukaryotes. Like, other chaperonins, it assists the folding of newly synthesised proteins., It is, however, unique in its specificity towards only a small subset of, non-native proteins. We determined two crystal structures of mouse, CCTgamma apical domain at 2.2 A and 2.8 A resolution. They reveal a, surface patch facing the inside of the torus that is highly evolutionarily, conserved and specific for the CCTgamma apical domain. This putative, substrate-binding region consists of predominantly positively charged, side-chains. It suggests that the specificity of this apical domain, towards its substrate, partially folded tubulin, is conferred by polar and, electrostatic interactions. The site and nature of substrate interaction, are thus profoundly different between CCT and its eubacterial homologue, GroEL, consistent with their different functions in general versus, specific protein folding assistance.

The chaperonin containing TCP-1 (CCT, also known as TRiC) is the only member of the chaperonin family found in the cytosol of eukaryotes. Like other chaperonins, it assists the folding of newly synthesised proteins. It is, however, unique in its specificity towards only a small subset of non-native proteins. We determined two crystal structures of mouse CCTgamma apical domain at 2.2 A and 2.8 A resolution. They reveal a surface patch facing the inside of the torus that is highly evolutionarily conserved and specific for the CCTgamma apical domain. This putative substrate-binding region consists of predominantly positively charged side-chains. It suggests that the specificity of this apical domain towards its substrate, partially folded tubulin, is conferred by polar and electrostatic interactions. The site and nature of substrate interaction are thus profoundly different between CCT and its eubacterial homologue GroEL, consistent with their different functions in general versus specific protein folding assistance.

==About this Structure==

Line 14:

[[Category: Single protein]]

[[Category: Pappenberger, G.]]

[[Category: Pearl, L.H.]]

[[Category: Pearl, L H.]]

[[Category: Roe, S.M.]]

[[Category: Roe, S M.]]

[[Category: Willison, K.R.]]

[[Category: Willison, K R.]]

[[Category: Wilsher, J.]]

[[Category: GOL]]

Line 24:

[[Category: tubulin]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun~~ Feb ~~3 09~~:41:02 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:39 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-The chaperonin containing TCP-1 (CCT, also known as TRiC) is the only, member of the chaperonin family found in the cytosol of eukaryotes. Like, other chaperonins, it assists the folding of newly synthesised proteins., It is, however, unique in its specificity towards only a small subset of, non-native proteins. We determined two crystal structures of mouse, CCTgamma apical domain at 2.2 A and 2.8 A resolution. They reveal a, surface patch facing the inside of the torus that is highly evolutionarily, conserved and specific for the CCTgamma apical domain. This putative, substrate-binding region consists of predominantly positively charged, side-chains. It suggests that the specificity of this apical domain, towards its substrate, partially folded tubulin, is conferred by polar and, electrostatic interactions. The site and nature of substrate interaction, are thus profoundly different between CCT and its eubacterial homologue, GroEL, consistent with their different functions in general versus, specific protein folding assistance.
+The chaperonin containing TCP-1 (CCT, also known as TRiC) is the only member of the chaperonin family found in the cytosol of eukaryotes. Like other chaperonins, it assists the folding of newly synthesised proteins. It is, however, unique in its specificity towards only a small subset of non-native proteins. We determined two crystal structures of mouse CCTgamma apical domain at 2.2 A and 2.8 A resolution. They reveal a surface patch facing the inside of the torus that is highly evolutionarily conserved and specific for the CCTgamma apical domain. This putative substrate-binding region consists of predominantly positively charged side-chains. It suggests that the specificity of this apical domain towards its substrate, partially folded tubulin, is conferred by polar and electrostatic interactions. The site and nature of substrate interaction are thus profoundly different between CCT and its eubacterial homologue GroEL, consistent with their different functions in general versus specific protein folding assistance.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Pappenberger, G.]]
-[[Category: Pearl, L.H.]]
+[[Category: Pearl, L H.]]
-[[Category: Roe, S.M.]]
+[[Category: Roe, S M.]]
-[[Category: Willison, K.R.]]
+[[Category: Willison, K R.]]
 [[Category: Wilsher, J.]]
 [[Category: GOL]]
@@ Line 24: / Line 24: @@
 [[Category: tubulin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:41:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:39 2008''