PDBsum entry 1sol

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Actin-binding protein PDB id
Protein chain
20 a.a.
PDB id:
Name: Actin-binding protein
Title: A pip2 and f-actin-binding site of gelsolin, residue 150- 169 (nmr, averaged structure)
Structure: Gelsolin (150-169). Chain: a
Source: not given
NMR struc: 1 models
Authors: W.Xian,R.Vegners,P.A.Janmey,W.H.Braunlin
Key ref: W.Xian et al. (1995). Spectroscopic studies of a phosphoinositide-binding peptide from gelsolin: behavior in solutions of mixed solvent and anionic micelles. Biophys J, 69, 2695-2702. PubMed id: 8599675
29-Sep-95     Release date:   08-Mar-96    
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Protein chain
Pfam   ArchSchema ?
P06396  (GELS_HUMAN) -  Gelsolin
782 a.a.
20 a.a.
Key:    PfamA domain  Secondary structure


Biophys J 69:2695-2702 (1995)
PubMed id: 8599675  
Spectroscopic studies of a phosphoinositide-binding peptide from gelsolin: behavior in solutions of mixed solvent and anionic micelles.
W.Xian, R.Vegners, P.A.Janmey, W.H.Braunlin.
The peptide G(150-169) corresponds to a phosphatidylinositol 4,5-bisphosphate (PIP2) and filamentous actin (F-actin) binding site on gelsolin (residues 150-169, with the sequence KHVVPNEVVVQRLFQVKGRR). The conformation of this peptide in trifluoroethanol (TFE) aqueous solution was determined by 1H nuclear magnetic resonance as the first step toward understanding the structural aspects of the interaction of G(150-169) and PIP2. The circular dichroism experiments show that G(150-169) adopts a predominantly alpha-helical form in both 50% TFE aqueous solution and in the presence of PIP2 micelles, therefore establishing a connection between the two conformations. 1H nuclear magnetic resonance experiments of G(150-169) in TFE co-solvent show that the helical region extends from Pro-154 to Lys-166. The amphiphilic nature of this helical structure may be the key to understanding the binding of the peptide to lipids. Sodium dodecyl sulfate micelle solution is used as a model for anionic lipid environments. Preliminary studies of the conformation of G(150-169) in sodium dodecyl sulfate micelle solution show that the peptide forms an alpha-helix similar to but with some structural differences from that in TFE co-solvent. Fluorescence experiments provide evidence of peptide clustering over a narrow range of peptide/PIP2 ratios, which is potentially relevant to the biological function of PIP2.

Literature references that cite this PDB file's key reference

  PubMed id Reference
16940084 R.Bucki, and P.A.Janmey (2006).
Interaction of the gelsolin-derived antibacterial PBP 10 peptide with lipid bilayers and cell membranes.
  Antimicrob Agents Chemother, 50, 2932-2940.  
15366709 P.A.Janmey, and U.Lindberg (2004).
Cytoskeletal regulation: rich in lipids.
  Nat Rev Mol Cell Biol, 5, 658-666.  
15105101 R.Bucki, J.J.Pastore, P.Randhawa, R.Vegners, D.J.Weiner, and P.A.Janmey (2004).
Antibacterial activities of rhodamine B-conjugated gelsolin-derived peptides compared to those of the antimicrobial peptides cathelicidin LL37, magainin II, and melittin.
  Antimicrob Agents Chemother, 48, 1526-1533.  
12712500 I.Liepi┼ća, C.Czaplewski, P.Janmey, and A.Liwo (2003).
Molecular dynamics study of a gelsolin-derived peptide binding to a lipid bilayer containing phosphatidylinositol 4,5-bisphosphate.
  Biopolymers, 71, 49-70.  
12186856 A.E.Wurmser, and S.D.Emr (2002).
Novel PtdIns(3)P-binding protein Etf1 functions as an effector of the Vps34 PtdIns 3-kinase in autophagy.
  J Cell Biol, 158, 761-772.  
11226199 R.C.Robinson, S.Choe, and L.D.Burtnick (2001).
The disintegration of a molecule: the role of gelsolin in FAF, familial amyloidosis (Finnish type).
  Proc Natl Acad Sci U S A, 98, 2117-2118.  
10801334 R.Bucki, F.Giraud, and J.C.Sulpice (2000).
Phosphatidylinositol 4,5-bisphosphate domain inducers promote phospholipid transverse redistribution in biological membranes.
  Biochemistry, 39, 5838-5844.  
10429191 E.K.Tuominen, J.M.Holopainen, J.Chen, G.D.Prestwich, P.R.Bachiller, P.K.Kinnunen, and P.A.Janmey (1999).
Fluorescent phosphoinositide derivatives reveal specific binding of gelsolin and other actin regulatory proteins to mixed lipid bilayers.
  Eur J Biochem, 263, 85-92.  
10810928 P.A.Janmey, W.Xian, and L.A.Flanagan (1999).
Controlling cytoskeleton structure by phosphoinositide-protein interactions: phosphoinositide binding protein domains and effects of lipid packing.
  Chem Phys Lipids, 101, 93.  
9533689 A.McGough, W.Chiu, and M.Way (1998).
Determination of the gelsolin binding site on F-actin: implications for severing and capping.
  Biophys J, 74, 764-772.  
9571211 P.A.Janmey, T.P.Stossel, and P.G.Allen (1998).
Deconstructing gelsolin: identifying sites that mimic or alter binding to actin and phosphoinositides.
  Chem Biol, 5, R81-R85.  
9665728 R.P.Johnson, V.Niggli, P.Durrer, and S.W.Craig (1998).
A conserved motif in the tail domain of vinculin mediates association with and insertion into acidic phospholipid bilayers.
  Biochemistry, 37, 10211-10222.  
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.