1nte: Difference between revisions

Line 4:

==Overview==

Crystal structures of the PDZ2 domain of the scaffolding protein syntenin, both unbound and in complexes with peptides derived from C termini of IL5, receptor (alpha chain) and syndecan, reveal the molecular roots of, syntenin's degenerate specificity. Three distinct binding sites (S(0), S(-1), and S(-2)), with affinities for hydrophobic side chains, function, in a combinatorial way: S(-1) and S(-2) act together to bind syndecan, while S(0) and S(-1) are involved in the binding of IL5Ralpha. Neither, mode of interaction is consistent with the prior classification scheme, which defined the IL5Ralpha interaction as class I (-S/T-X-phi) and the, syndecan interaction as class II (-phi-X-phi). These results, in, conjunction with other emerging structural data on PDZ domains, call for a, revision of their classification and of the existing model of their, mechanism.

Crystal structures of the PDZ2 domain of the scaffolding protein syntenin, both unbound and in complexes with peptides derived from C termini of IL5 receptor (alpha chain) and syndecan, reveal the molecular roots of syntenin's degenerate specificity. Three distinct binding sites (S(0), S(-1), and S(-2)), with affinities for hydrophobic side chains, function in a combinatorial way: S(-1) and S(-2) act together to bind syndecan, while S(0) and S(-1) are involved in the binding of IL5Ralpha. Neither mode of interaction is consistent with the prior classification scheme, which defined the IL5Ralpha interaction as class I (-S/T-X-phi) and the syndecan interaction as class II (-phi-X-phi). These results, in conjunction with other emerging structural data on PDZ domains, call for a revision of their classification and of the existing model of their mechanism.

==About this Structure==

Line 15:

[[Category: Cooper, D.]]

[[Category: Derewenda, U.]]

[[Category: Derewenda, Z.S.]]

[[Category: Derewenda, Z S.]]

[[Category: Devedjiev, Y.]]

[[Category: Kang, B.S.]]

[[Category: Kang, B S.]]

[[Category: O]]

[[Category: pdz recognition]]

[[Category: syntenin]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 16~~:30:45 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:50 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-Crystal structures of the PDZ2 domain of the scaffolding protein syntenin, both unbound and in complexes with peptides derived from C termini of IL5, receptor (alpha chain) and syndecan, reveal the molecular roots of, syntenin's degenerate specificity. Three distinct binding sites (S(0), S(-1), and S(-2)), with affinities for hydrophobic side chains, function, in a combinatorial way: S(-1) and S(-2) act together to bind syndecan, while S(0) and S(-1) are involved in the binding of IL5Ralpha. Neither, mode of interaction is consistent with the prior classification scheme, which defined the IL5Ralpha interaction as class I (-S/T-X-phi) and the, syndecan interaction as class II (-phi-X-phi). These results, in, conjunction with other emerging structural data on PDZ domains, call for a, revision of their classification and of the existing model of their, mechanism.
+Crystal structures of the PDZ2 domain of the scaffolding protein syntenin, both unbound and in complexes with peptides derived from C termini of IL5 receptor (alpha chain) and syndecan, reveal the molecular roots of syntenin's degenerate specificity. Three distinct binding sites (S(0), S(-1), and S(-2)), with affinities for hydrophobic side chains, function in a combinatorial way: S(-1) and S(-2) act together to bind syndecan, while S(0) and S(-1) are involved in the binding of IL5Ralpha. Neither mode of interaction is consistent with the prior classification scheme, which defined the IL5Ralpha interaction as class I (-S/T-X-phi) and the syndecan interaction as class II (-phi-X-phi). These results, in conjunction with other emerging structural data on PDZ domains, call for a revision of their classification and of the existing model of their mechanism.
 ==About this Structure==
@@ Line 15: / Line 15: @@
 [[Category: Cooper, D.]]
 [[Category: Derewenda, U.]]
-[[Category: Derewenda, Z.S.]]
+[[Category: Derewenda, Z S.]]
 [[Category: Devedjiev, Y.]]
-[[Category: Kang, B.S.]]
+[[Category: Kang, B S.]]
 [[Category: O]]
 [[Category: pdz recognition]]
 [[Category: syntenin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:30:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:50 2008''