HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Life Science / Faculty of Advanced Life Science >
Peer-reviewed Journal Articles, etc >

Nrp1 is Activated by Konjac Ceramide Binding-Induced Structural Rigidification of the a1a2 Domain

This item is licensed under: Creative Commons Attribution 4.0 International

Files in This Item:

The file(s) associated with this item can be obtained from the following URL:https://doi.org/10.3390/cells9020517


Title: Nrp1 is Activated by Konjac Ceramide Binding-Induced Structural Rigidification of the a1a2 Domain
Authors: Usuki, Seigo Browse this author
Yasutake, Yoshiaki Browse this author
Tamura, Noriko Browse this author
Tamura, Tomohiro Browse this author
Tanji, Kunikazu Browse this author
Saitoh, Takashi Browse this author
Murai, Yuta Browse this author
Mikami, Daisuke Browse this author
Yuyama, Kohei Browse this author
Monde, Kenji Browse this author
Mukai, Katsuyuki Browse this author
Igarashi, Yasuyuki Browse this author →KAKEN DB
Keywords: ceramide
konjac
semaphorin3A
neurite outgrowth
neuropilin 1
endoglycoceramidase
sphingadienine
Issue Date: Feb-2020
Publisher: MDPI
Journal Title: Cells
Volume: 9
Issue: 2
Start Page: 517
Publisher DOI: 10.3390/cells9020517
Abstract: Konjac ceramide (kCer) is a plant-type ceramide composed of various long-chain bases and alpha-hydroxyl fatty acids. The presence of d4t,8t-sphingadienine is essential for semaphorin 3A (Sema3A)-like activity. Herein, we examined the three neuropilin 1 (Nrp1) domains (a1a2, b1b2, or c), and found that a1a2 binds to d4t,8t-kCer and possesses Sema3A-like activity. kCer binds to Nrp1 with a weak affinity of mu M dissociation constant (Kd). We wondered whether bovine serum albumin could influence the ligand-receptor interaction that a1a2 has with a single high affinity binding site for kCer (Kd in nM range). In the present study we demonstrated the influence of bovine serum albumin. Thermal denaturation indicates that the a1a2 domain may include intrinsically disordered region (IDR)-like flexibility. A potential interaction site on the a1 module was explored by molecular docking, which revealed a possible Nrp1 activation mechanism, in which kCer binds to Site A close to the Sema3A-binding region of the a1a2 domain. The a1 module then accesses a2 as the IDR-like flexibility becomes ordered via kCer-induced protein rigidity of a1a2. This induces intramolecular interaction between a1 and a2 through a slight change in protein secondary structure.
Rights: https://creativecommons.org/licenses/by/4.0/
Type: article
URI: http://hdl.handle.net/2115/78370
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Export metadata:

OAI-PMH ( junii2 , jpcoar )

MathJax is now OFF:


 

 - Hokkaido University