Secondary structure and 1H, 13C, 15N resonance assignments of the endosomal sorting protein sorting nexin 3

Michael Overduin; Sandya Rajesh; Jean Gruenberg; Marc Lenoir

doi:10.1007/s12104-015-9609-z

Secondary structure and 1H, 13C, 15N resonance assignments of the endosomal sorting protein sorting nexin 3

Michael Overduin, Sandya Rajesh, Jean Gruenberg, Marc Lenoir

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4 Citations (Scopus)

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Abstract

Sorting nexin 3 (SNX3) belongs to a sub-family of sorting nexins that primarily contain a single Phox homology domain capable of binding phosphoinositides and membranes. We report the complete 1H, 13C and 15N resonance assignments of the full-length human SNX3 protein and identification of its secondary structure elements, revealing a canonical fold and unstructured termini.

Original language	English
Journal	Biomolecular NMR Assignments
Early online date	19 Apr 2015
DOIs	https://doi.org/10.1007/s12104-015-9609-z
Publication status	Published - 2015

Keywords

SNX3
PX domain
Phosphoinositide recognition
Phosphatidylinositol 3-phosphate
Endosome
NMR

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10.1007/s12104-015-9609-z

Overduin_et_al_Secondary_structure_Biomolecular_NMR_Assignments_2015
Eligibility for repository : checked 23/06/2015
Final published version, 667 KBLicence: Creative Commons: Attribution (CC BY)

http://link.springer.com/10.1007/s12104-015-9609-z

Structure-aided Discovery of CaMK1D Kinase Inhibitors as Targeted Therapeutic Agents for Breast Cancer (CAMSEED)
Butterworth, S. (Principal Investigator), Berditchevski, F. (Co-Investigator) & Overduin, M. (Co-Investigator)
Wellcome Trust
1/07/14 → 31/01/17
Project: Research
(36MTHS)Structural Basis of Membrane Trafficking and Signalling Interactions of Proteins Implicated in Cancer Progression
Overduin, M. (Principal Investigator)
Cancer Research UK
1/02/11 → 31/01/14
Project: Research

Cite this

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title = "Secondary structure and 1H, 13C, 15N resonance assignments of the endosomal sorting protein sorting nexin 3",

abstract = "Sorting nexin 3 (SNX3) belongs to a sub-family of sorting nexins that primarily contain a single Phox homology domain capable of binding phosphoinositides and membranes. We report the complete 1H, 13C and 15N resonance assignments of the full-length human SNX3 protein and identification of its secondary structure elements, revealing a canonical fold and unstructured termini.",

keywords = "SNX3, PX domain , Phosphoinositide recognition, Phosphatidylinositol 3-phosphate, Endosome, NMR",

author = "Michael Overduin and Sandya Rajesh and Jean Gruenberg and Marc Lenoir",

year = "2015",

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language = "English",

journal = "Biomolecular NMR Assignments",

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AU - Overduin, Michael

AU - Rajesh, Sandya

AU - Gruenberg, Jean

AU - Lenoir, Marc

PY - 2015

Y1 - 2015

N2 - Sorting nexin 3 (SNX3) belongs to a sub-family of sorting nexins that primarily contain a single Phox homology domain capable of binding phosphoinositides and membranes. We report the complete 1H, 13C and 15N resonance assignments of the full-length human SNX3 protein and identification of its secondary structure elements, revealing a canonical fold and unstructured termini.

AB - Sorting nexin 3 (SNX3) belongs to a sub-family of sorting nexins that primarily contain a single Phox homology domain capable of binding phosphoinositides and membranes. We report the complete 1H, 13C and 15N resonance assignments of the full-length human SNX3 protein and identification of its secondary structure elements, revealing a canonical fold and unstructured termini.

KW - SNX3

KW - PX domain

KW - Phosphoinositide recognition

KW - Phosphatidylinositol 3-phosphate

KW - Endosome

KW - NMR

U2 - 10.1007/s12104-015-9609-z

DO - 10.1007/s12104-015-9609-z

M3 - Article

C2 - 25893673

SN - 1874-2718

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

ER -

Secondary structure and 1H, 13C, 15N resonance assignments of the endosomal sorting protein sorting nexin 3

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Projects

Structure-aided Discovery of CaMK1D Kinase Inhibitors as Targeted Therapeutic Agents for Breast Cancer (CAMSEED)

(36MTHS)Structural Basis of Membrane Trafficking and Signalling Interactions of Proteins Implicated in Cancer Progression

Cite this