Structural highlights
Publication Abstract from PubMed
NESCA, a newly discovered signaling adapter protein in the NGF-pathway, contains a RUN domain at its N-terminus. Here we report the crystal structure of the NESCA RUN domain determined at 2.0-A resolution. The overall fold of the NESCA RUN domain comprises nine helices, resembling the RUN domain of RPIPx and the RUN1 domain of Rab6IP1. However, compared to the other RUN domains, the RUN domain of NESCA has significantly different surface electrostatic distributions at the putative GTPase-interacting interface. We demonstrate that the RUN domain of NESCA can bind H-Ras, a downstream signaling molecule of TrkA, with high affinity. Moreover, NESCA RUN can directly interact with TrkA. These results provide new insights into how NESCA participates in the NGF-TrkA signaling pathway.
Crystal structure and functional implication of the RUN domain of human NESCA.,Sun Q, Han C, Liu L, Wang Y, Deng H, Bai L, Jiang T Protein Cell. 2012 Aug;3(8):609-17. Epub 2012 Jul 22. PMID:22821014[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sun Q, Han C, Liu L, Wang Y, Deng H, Bai L, Jiang T. Crystal structure and functional implication of the RUN domain of human NESCA. Protein Cell. 2012 Aug;3(8):609-17. Epub 2012 Jul 22. PMID:22821014 doi:10.1007/s13238-012-2052-3
