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PDBsum entry 1nsh

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protein Protein-protein interface(s) links
Metal binding protein PDB id
1nsh
Jmol
Contents
Protein chains
101 a.a. *
* Residue conservation analysis
PDB id:
1nsh
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
Date:
27-Jan-03     Release date:   15-Jul-03    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P24480  (S10AB_RABIT) -  Protein S100-A11
Seq:
Struc:
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.
 
  ABSTRACT  
 
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.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.