1H, 15N, 13C resonance assignment of human GAP-43

Andrea Gabriele Flamm; Szymon Żerko; Anna Zawadzka-Kazimierczuk; Wiktor Koźmiński; Robert Konrat; Nicolas Coudevylle

doi:10.1007/s12104-015-9660-9

1H, 15N, 13C resonance assignment of human GAP-43

Biomol NMR Assign. 2016 Apr;10(1):171-4. doi: 10.1007/s12104-015-9660-9. Epub 2016 Jan 9.

Authors

Andrea Gabriele Flamm¹, Szymon Żerko², Anna Zawadzka-Kazimierczuk², Wiktor Koźmiński², Robert Konrat¹, Nicolas Coudevylle³

Affiliations

¹ Department of Computational and Structural Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria.
² Faculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, Żwirki i Wigury 101, 02-089, Warsaw, Poland.
³ Department of Computational and Structural Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria. nicolas.coudevylle@univie.ac.at.

Abstract

GAP-43 is a 25 kDa neuronal intrinsically disordered protein, highly abundant in the neuronal growth cone during development and regeneration. The exact molecular function(s) of GAP-43 remains unclear but it appears to be involved in growth cone guidance and actin cytoskeleton organization. Therefore, GAP-43 seems to play an important role in neurotransmitter vesicle fusion and recycling, long-term potentiation, spatial memory formation and learning. Here we report the nearly complete assignment of recombinant human GAP-43.

Keywords: GAP-43; Growth cone; Intrinsically disordered protein; Neuromodulin.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cell Membrane / metabolism
GAP-43 Protein / chemistry*
GAP-43 Protein / metabolism
Humans
Ligands
Nuclear Magnetic Resonance, Biomolecular

Substances

GAP-43 Protein
Ligands