1A4P

P11 (S100A10), LIGAND OF ANNEXIN II

Summary for 1A4P

• Entry DOI: 10.2210/pdb1a4p/pdb
• Descriptor: S100A10 (2 entities in total)
• Functional Keywords: s100 family, ef-hand protein, ligand of annexin ii, calcium/phospholipid binding protein, calcium-phospholipid binding protein complex
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 22177.88

Authors

Rety, S.,Sopkova, J.,Renouard, M.,Osterloh, D.,Gerke, V.,Russo-Marie, F.,Lewit-Bentley, A. (deposition date: 1998-01-30, release date: 1998-05-27, Last modification date: 2011-07-13)

Primary citation

Rety, S.,Sopkova, J.,Renouard, M.,Osterloh, D.,Gerke, V.,Tabaries, S.,Russo-Marie, F.,Lewit-Bentley, A.
The crystal structure of a complex of p11 with the annexin II N-terminal peptide.
Nat.Struct.Biol., 6:89-95, 1999

PubMed Abstract: 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.

PubMed: 9886297
DOI: 10.1038/4965

Experimental method

X-RAY DIFFRACTION (2.25 Å)