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1a4p
From Proteopedia
(New page: 200px<br /> <applet load="1a4p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a4p, resolution 2.25Å" /> '''P11 (S100A10), LIGA...) |
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| - | [[Image:1a4p.gif|left|200px]]<br /> | + | [[Image:1a4p.gif|left|200px]]<br /><applet load="1a4p" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1a4p" size=" | + | |
caption="1a4p, resolution 2.25Å" /> | caption="1a4p, resolution 2.25Å" /> | ||
'''P11 (S100A10), LIGAND OF ANNEXIN II'''<br /> | '''P11 (S100A10), LIGAND OF ANNEXIN II'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The aggregation and membrane fusion properties of annexin II are modulated | + | 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== | ==About this Structure== | ||
| - | 1A4P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1A4P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: s100 family]] | [[Category: s100 family]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:48 2008'' |
Revision as of 09:40, 21 February 2008
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P11 (S100A10), LIGAND OF ANNEXIN II
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.
About this Structure
1A4P is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of a complex of p11 with the annexin II N-terminal peptide., Rety S, Sopkova J, Renouard M, Osterloh D, Gerke V, Tabaries S, Russo-Marie F, Lewit-Bentley A, Nat Struct Biol. 1999 Jan;6(1):89-95. PMID:9886297
Page seeded by OCA on Thu Feb 21 11:40:48 2008
