1H, 13C and 15N resonance assignments of the human filamin A tandem immunoglobulin-like domains 16-17 and 18-19.
Filamins are large actin-binding and cross-linking proteins which act as linkers between the cytoskeleton and various signaling proteins. Filamin A (FLNa) is the most abundant of the three filamin isoforms found in humans. FLNa contains an N-terminal actin-binding domain and 24 immunoglobulin-like (Ig) domains. The Ig domains are responsible for the FLNa dimerization and most of the interactions that FLNa has with numerous other proteins. There are several crystal and solution structures from isolated single Ig domains of filamins in the PDB database, but only few from longer constructs. Here, we present nearly complete chemical shift assignments of FLNa tandem Ig domains 16-17 and 18-19. Chemical shift mapping between FLNa tandem Ig domain 16-17 and isolated domain 17 suggests a novel domain-domain interaction mode.
Heikkinen
Outi
O
Laboratory of Organic Chemistry, Department of Chemistry, University of Helsinki, A.I. Virtasen Aukio 1, P.O. Box 55, 00014, Helsinki, Finland. Outi.K.Heikkinen@helsinki.fi
Permi
Perttu
P
Koskela
Harri
H
Ylänne
Jari
J
Kilpeläinen
Ilkka
I
D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D003285:Contractile Proteins / Q000737:chemistry*; D064448:Filamins; D006801:Humans; D007074:Immunoglobulin G / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008840:Microfilament Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes / Q000737:chemistry; D011522:Protons
D002247:Carbon Isotopes; D003285:Contractile Proteins; D064448:Filamins; D007074:Immunoglobulin G; D008840:Microfilament Proteins; D009587:Nitrogen Isotopes; D011522:Protons