Article

Signature of N-terminal domain (NTD) structural re-orientation in NPC1 for proper alignment of cholesterol transport: Molecular dynamics study with mutation

2020-06-09

Abstract excerpt

The lysosomal membrane protein NPC1 (Niemann-Pick type C1) and NPC2 (Niemann-Pick type C2) are main players of cholesterol control in lysosome and it is known that mutation on these proteins leads to cholesterol trafficking related disease, called Niemann-Pick disease type C (NPC) disease. The mutation R518W or R518Q on NPC1 is one of such disease-related mutations, causing reduced cholesterol transport by half, r...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 1703c14a-a38e-5609-954e-4533c8b27b4a
DOI: 10.1101/2020.06.09.141630

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Signature of N-terminal domain (NTD) structural re-orientation in NPC1 for proper alignment of cholesterol transport: Molecular dynamics study with mutationDOI 10.1101/2020.06.09.141630Read

Molecular dynamics study with mutation shows that N-terminal domain structural re-orientation in Niemann-Pick type C1 is required for proper alignment of cholesterol transport.Semantic proximity Read

The point mutation of the cholesterol trafficking membrane protein NPC1 may affect its proper function in more than a single step: Molecular dynamics simulation study.Semantic proximity Read

3.3 Å structure of Niemann-Pick C1 protein reveals insights into the function of the C-terminal luminal domain in cholesterol transport.Semantic proximity Read

Cholesterol binding to the sterol-sensing region of Niemann Pick C1 protein confines dynamics of its N-terminal domainSemantic proximity Read

Molecular analysis of NPC1 and NPC2 gene in 34 Niemann-Pick C Italian patients: identification and structural modeling of novel mutations.Semantic proximity Read

The NPC1 protein: structure implies function.Semantic proximity Read

NPC1/NPC2 function as a tag team duo to mobilize cholesterolSemantic proximity Read

Microdynamics of lamin A Ig-fold domain regulates higher order assembly of the proteinSemantic proximity Read

Nucleoporin's Like Charge Regions Are Major Regulators of FG Coverage and Dynamics Inside the Nuclear Pore Complex.Semantic proximity Read

A new insight into protein-protein interactions and the effect of conformational alterations in PCNA.Semantic proximity Read

Computational insights of K1444N substitution in GAP-related domain of NF1 gene associated with neurofibromatosis type 1 disease: a molecular modeling and dynamics approach.Semantic proximity Read

Towards the NMR solution Structure and the Dynamics of the C-terminal Region of APOL1 and its G1, G2 Variants with a Membrane MimeticSemantic proximity Read