PDBsum entry 1nsh

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protein Protein-protein interface(s) links
Metal binding protein PDB id
Protein chains
101 a.a. *
* Residue conservation analysis
PDB id:
Name: Metal binding protein
Title: Solution structure of rabbit apo-s100a11 (19 models)
Structure: Calgizzarin. Chain: a, b. Synonym: s100c protein. Engineered: yes
Source: Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986. Gene: s100a11 or s100c or pcalg. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
NMR struc: 19 models
Authors: A.C.Dempsey,M.P.Walsh,G.S.Shaw
Key ref:
A.C.Dempsey et al. (2003). Unmasking the annexin I interaction from the structure of Apo-S100A11. Structure, 11, 887-897. PubMed id: 12842051 DOI: 10.1016/S0969-2126(03)00126-6
27-Jan-03     Release date:   15-Jul-03    
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Protein chains
Pfam   ArchSchema ?
P24480  (S10AB_RABIT) -  Protein S100-A11
102 a.a.
101 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular space   5 terms 
  Biological process     regulation of cell proliferation   1 term 
  Biochemical function     S100 protein binding     5 terms  


DOI no: 10.1016/S0969-2126(03)00126-6 Structure 11:887-897 (2003)
PubMed id: 12842051  
Unmasking the annexin I interaction from the structure of Apo-S100A11.
A.C.Dempsey, M.P.Walsh, G.S.Shaw.
S100A11 is a homodimeric EF-hand calcium binding protein that undergoes a calcium-induced conformational change and interacts with the phospholipid binding protein annexin I to coordinate membrane association. In this work, the solution structure of apo-S100A11 has been determined by NMR spectroscopy to uncover the details of its calcium-induced structural change. Apo-S100A11 forms a tight globular structure having a near antiparallel orientation of helices III and IV in calcium binding site II. Further, helices I and IV, and I and I', form a more closed arrangement than observed in other apo-S100 proteins. This helix arrangement in apo-S100A11 partially buries residues in helices I (P3, E11, A15), III (V55, R58, M59), and IV (A86, C87, S90) and the linker (A45, F46), which are required for interaction with annexin I in the calcium-bound state. In apo-S100A11, this results in a "masked" binding surface that prevents annexin I binding but is uncovered upon calcium binding.
  Selected figure(s)  
Figure 6.
Figure 6. Formation of the Annexin I Binding Surface from Calcium Binding to Apo-S100A11Accessible surface area representations of apo-S100A11 (A) and calcium-bound S100A11 (B) in complex with annexin I (Rety et al., 2000). Each protein is oriented approximately 90 with respect to that shown in Figure 4. In both molecules, residues in S100A11 that directly interact (<5 ) with annexin I are indicated and colored dark blue and those whose side chain exposure increases by >20% upon calcium binding but have less interaction are colored cyan. For apo-S100A11 (A), many of these residues have less than 20% of their side chains accessible to the surface and are disjoint on the surface of the protein. In the calcium-bound structure (B), most residues that contact the annexin I peptide increase their side chain-accessible surface areas by >20% as shown in Figure 5C to form a contiguous site for the annexin interaction (dark blue). To facilitate comparison, all sequence numbers correspond to those of rabbit S100A11.
  The above figure is reprinted by permission from Cell Press: Structure (2003, 11, 887-897) copyright 2003.  
  Figure was selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21269277 L.Santamaria-Kisiel, and G.S.Shaw (2011).
Identification of regions responsible for the open conformation of S100A10 using chimaeric S100A11-S100A10 proteins.
  Biochem J, 434, 37-48.  
19452629 N.T.Wright, B.R.Cannon, P.T.Wilder, M.T.Morgan, K.M.Varney, D.B.Zimmer, and D.J.Weber (2009).
Solution structure of S100A1 bound to the CapZ peptide (TRTK12).
  J Mol Biol, 386, 1265-1277.  
18795951 A.C.Rintala-Dempsey, A.Rezvanpour, and G.S.Shaw (2008).
S100-annexin complexes--structural insights.
  FEBS J, 275, 4956-4966.  
17978094 M.Sakaguchi, H.Sonegawa, H.Murata, M.Kitazoe, J.Futami, K.Kataoka, H.Yamada, and N.H.Huh (2008).
S100A11, an Dual Mediator for Growth Regulation of Human Keratinocytes.
  Mol Biol Cell, 19, 78-85.  
18384084 S.Malik, M.Revington, S.P.Smith, and G.S.Shaw (2008).
Analysis of the structure of human apo-S100B at low temperature indicates a unimodal conformational distribution is adopted by calcium-free S100 proteins.
  Proteins, 73, 28-42.
PDB code: 2pru
18618420 T.Kouno, M.Mizuguchi, M.Sakaguchi, E.Makino, Y.Mori, H.Shinoda, T.Aizawa, M.Demura, N.H.Huh, and K.Kawano (2008).
The structure of S100A11 fragment explains a local structural change induced by phosphorylation.
  J Pept Sci, 14, 1129-1138.  
18410126 V.N.Malashkevich, K.M.Varney, S.C.Garrett, P.T.Wilder, D.Knight, T.H.Charpentier, U.A.Ramagopal, S.C.Almo, D.J.Weber, and A.R.Bresnick (2008).
Structure of Ca2+-bound S100A4 and its interaction with peptides derived from nonmuscle myosin-IIA.
  Biochemistry, 47, 5111-5126.
PDB code: 2q91
17714509 T.Uebi, N.Miwa, and S.Kawamura (2007).
Comprehensive interaction of dicalcin with annexins in frog olfactory and respiratory cilia.
  FEBS J, 274, 4863-4876.  
12842036 S.Bhattacharya, and W.J.Chazin (2003).
Calcium-driven changes in S100A11 structure revealed.
  Structure, 11, 738-740.  
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