1bt6: Difference between revisions

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==Overview==

The aggregation and membrane fusion properties of annexin II are modulated, by the association with a regulatory light chain called p11.p11 is a, member of the S100 EF-hand protein family, which is unique in having lost, its calcium-binding properties. We report the first structure of a complex, between p11 and its cognate peptide, the N-terminus of annexin II, as well, as that of p11 alone. The basic unit for p11 is a tight, non-covalent, dimer. In the complex, each annexin II peptide forms hydrophobic, interactions with both p11 monomers, thus providing a structural basis for, high affinity interactions between an S100 protein and its target, sequence. Finally, p11 forms a disulfide-linked tetramer in both types of, crystals thus suggesting a model for an oxidized form of other S100, proteins that have been found in the extracellular milieu.

The aggregation and membrane fusion properties of annexin II are modulated by the association with a regulatory light chain called p11.p11 is a member of the S100 EF-hand protein family, which is unique in having lost its calcium-binding properties. We report the first structure of a complex between p11 and its cognate peptide, the N-terminus of annexin II, as well as that of p11 alone. The basic unit for p11 is a tight, non-covalent dimer. In the complex, each annexin II peptide forms hydrophobic interactions with both p11 monomers, thus providing a structural basis for high affinity interactions between an S100 protein and its target sequence. Finally, p11 forms a disulfide-linked tetramer in both types of crystals thus suggesting a model for an oxidized form of other S100 proteins that have been found in the extracellular milieu.

==About this Structure==

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[[Category: s100 family]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 15~~:33:21 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:54 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The aggregation and membrane fusion properties of annexin II are modulated, by the association with a regulatory light chain called p11.p11 is a, member of the S100 EF-hand protein family, which is unique in having lost, its calcium-binding properties. We report the first structure of a complex, between p11 and its cognate peptide, the N-terminus of annexin II, as well, as that of p11 alone. The basic unit for p11 is a tight, non-covalent, dimer. In the complex, each annexin II peptide forms hydrophobic, interactions with both p11 monomers, thus providing a structural basis for, high affinity interactions between an S100 protein and its target, sequence. Finally, p11 forms a disulfide-linked tetramer in both types of, crystals thus suggesting a model for an oxidized form of other S100, proteins that have been found in the extracellular milieu.
+The aggregation and membrane fusion properties of annexin II are modulated by the association with a regulatory light chain called p11.p11 is a member of the S100 EF-hand protein family, which is unique in having lost its calcium-binding properties. We report the first structure of a complex between p11 and its cognate peptide, the N-terminus of annexin II, as well as that of p11 alone. The basic unit for p11 is a tight, non-covalent dimer. In the complex, each annexin II peptide forms hydrophobic interactions with both p11 monomers, thus providing a structural basis for high affinity interactions between an S100 protein and its target sequence. Finally, p11 forms a disulfide-linked tetramer in both types of crystals thus suggesting a model for an oxidized form of other S100 proteins that have been found in the extracellular milieu.
 ==About this Structure==
@@ Line 27: / Line 27: @@
 [[Category: s100 family]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:33:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:54 2008''