From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1qls.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1qls.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1qls| PDB=1qls | SCENE= }} | | {{STRUCTURE_1qls| PDB=1qls | SCENE= }} |
| | | | |
| - | '''S100C (S100A11),OR CALGIZZARIN, IN COMPLEX WITH ANNEXIN I N-TERMINUS'''
| + | ===S100C (S100A11),OR CALGIZZARIN, IN COMPLEX WITH ANNEXIN I N-TERMINUS=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Background: S100C (S100A11) is a member of the S100 calcium-binding protein family, the function of which is not yet entirely clear, but may include cytoskeleton assembly and dynamics. S100 proteins consist of two EF-hand calcium-binding motifs, connected by a flexible loop. Like several other members of the family, S100C forms a homodimer. A number of S100 proteins form complexes with annexins, another family of calcium-binding proteins that also bind to phospholipids. Structural studies have been undertaken to understand the basis of these interactions. Results: We have solved the crystal structure of a complex of calcium-loaded S100C with a synthetic peptide that corresponds to the first 14 residues of the annexin I N terminus at 2.3 A resolution. We find a stoichiometry of one peptide per S100C monomer, the entire complex structure consisting of two peptides per S100C dimer. Each peptide, however, interacts with both monomers of the S100C dimer. The two S100C molecules of the dimer are linked by a disulphide bridge. The structure is surprisingly close to that of the p11-annexin II N-terminal peptide complex solved previously. We have performed competition experiments to try to understand the specificity of the S100-annexin interaction. Conclusions: By solving the structure of a second annexin N terminus-S100 protein complex, we confirmed a novel mode of interaction of S100 proteins with their target peptides; there is a one-to-one stoichiometry, where the dimeric structure of the S100 protein is, nevertheless, essential for complex formation. Our structure can provide a model for a Ca(2+)-regulated annexin I-S100C heterotetramer, possibly involved in crosslinking membrane surfaces or organising membranes during certain fusion events.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10673436}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10673436 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_10673436}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 34: |
Line 38: |
| | [[Category: Ligand of annexin ii]] | | [[Category: Ligand of annexin ii]] |
| | [[Category: S100 family]] | | [[Category: S100 family]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:25:33 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:09:02 2008'' |
Revision as of 10:09, 27 July 2008
Template:STRUCTURE 1qls
S100C (S100A11),OR CALGIZZARIN, IN COMPLEX WITH ANNEXIN I N-TERMINUS
Template:ABSTRACT PUBMED 10673436
About this Structure
1QLS is a Protein complex structure of sequences from Homo sapiens and Sus scrofa. Full crystallographic information is available from OCA.
Reference
Structural basis of the Ca(2+)-dependent association between S100C (S100A11) and its target, the N-terminal part of annexin I., Rety S, Osterloh D, Arie JP, Tabaries S, Seeman J, Russo-Marie F, Gerke V, Lewit-Bentley A, Structure. 2000 Feb 15;8(2):175-84. PMID:10673436
Page seeded by OCA on Sun Jul 27 13:09:02 2008
