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PDBsum entry 2k8m

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protein Protein-protein interface(s) links
Protein transport PDB id
2k8m
Jmol
Contents
Protein chains
128 a.a. *
98 a.a. *
* Residue conservation analysis
PDB id:
2k8m
Name: Protein transport
Title: S100a13-c2a binary complex structure
Structure: Putative uncharacterized protein. Chain: a, d. Fragment: residues 1-128. Synonym: syt1. Engineered: yes. Protein s100-a13. Chain: b, c. Synonym: s100 calcium-binding protein a13. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: dkfzp781d2042, hcg_2016754, syt1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: s100a13.
NMR struc: 20 models
Authors: S.K.Mohan,S.G.Rani,S.M.Kumar,C.Yu
Key ref: S.K.Mohan et al. (2009). S100A13-C2A binary complex structure-a key component in the acidic fibroblast growth factor for the non-classical pathway. Biochem Biophys Res Commun, 380, 514-519. PubMed id: 19284995 DOI: 10.1016/j.bbrc.2009.01.143
Date:
14-Sep-08     Release date:   17-Mar-09    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P21579  (SYT1_HUMAN) -  Synaptotagmin-1
Seq:
Struc:
422 a.a.
128 a.a.
Protein chains
Pfam   ArchSchema ?
Q99584  (S10AD_HUMAN) -  Protein S100-A13
Seq:
Struc:
98 a.a.
98 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   10 terms 
  Biological process     transport   10 terms 
  Biochemical function     transporter activity     10 terms  

 

 
DOI no: 10.1016/j.bbrc.2009.01.143 Biochem Biophys Res Commun 380:514-519 (2009)
PubMed id: 19284995  
 
 
S100A13-C2A binary complex structure-a key component in the acidic fibroblast growth factor for the non-classical pathway.
S.K.Mohan, S.G.Rani, S.M.Kumar, C.Yu.
 
  ABSTRACT  
 
Fibroblast growth factors (FGFs) are key regulators of cell proliferation, differentiation, tumor-induced angiogenesis and migration. FGFs are essential for early embryonic development, organ formation and angiogenesis. They play important roles in tumor formation, inflammation, wound healing and restenosis. The biological effects of FGFs are mediated through the activation of the four transmembrane phosphotyrosine kinase receptors (FGFRs) in the presence of heparin sulfate proteoglycans (HSPGs) and therefore require the release of FGFs into the extracellular space. However, FGF-1 lacks the signal peptide required for the releasing of these proteins through the classical endoplasmic reticulum (ER)-Golgi secretary pathway. Maciag et al. demonstrated that FGF-1 is exported through a non-classical release pathway involving the formation of a specific multiprotein complex [M. Landriscina, R. Soldi, C. Bagala, I. Micucci, S. Bellum, F. Tarantini, I. Prudovsky, T. Maciag, S100A13 participates in the release of fibroblast growth factor 1 in response to heat shock in vitro, J. Biol. Chem. 276 (2001) 22544-22552; C.M. Carreira, T.M. LaVallee, F. Tarantini, A. Jackson, J.T. Lathrop, B. Hampton, W.H. Burgess, T. Maciag, S100A13 is involved in the regulation of fibroblast growth factor-1 and p40 synaptotagmin-1 release in vitro, J. Biol. Chem. 273 (1998) 22224-22231; T.M. LaValle, F. Tarantini, S. Gamble, C.M. Carreira, A. Jackson, T. Maciag, Synaptotagmin-1 is required for fibroblast growth factor-1 release, J. Biol. Chem. 273 (1998) 22217-22223; C. Bagalá, V. Kolev, A. Mandinova, R. Soldi, C. Mouta, I. Graziani, I, Prudovsky, T. Maciag, The alternative translation of synaptotagmin 1 mediates the non-classical release of FGF1, Biochem. Biophys. Res. Commun. 310 (2003) 1041-1047]. The protein constituents of this complex include FGF-1, S100A13 (a Ca(2+)-binding protein), and the p40 form of synaptotagmin 1 (Syt1). To understand the molecular events in the FGF-1 releasing pathway, we have studied the interactions of S100A13 with C2A by (1)H-(15)N HSQC titration and 3D-filtered NOESY experiments. We characterized the binary complex structure of S100A13-C2A by using a variety of multi-dimensional NMR experiments. This complex acts as a template for FGF-1 dimerization and multiprotein complex formation.