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a(HBP:HBP00170)

Equivalencies: 0 | Classes: 0 | Children: 0 | Explore

Entity

Name
HBP00170
Namespace
HBP
Namespace Version
20181029
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/785431732a26d6809b4162d98b95687d16404e63/export/hbp.belns

Appears in Networks 1

Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau v1.0.0

In-Edges 5

complex(a(GO:"filamentous actin"), p(HGNC:MAPT, frag("261_265"))) increases a(HBP:HBP00170) View Subject | View Object

The analysis suggests that the experimental NOE data witness the formation of helical structure in these regions upon binding to F-actin, but the number of detected restraints is not sufficient to define a unique conformation PubMed:29215007

Appears in Networks:
Annotations
Confidence
High

p(HGNC:MAPT, frag("261_265")) increases a(HBP:HBP00170) View Subject | View Object

In some of the other conformers of Tau (254–290), however, residues 261–265 were identified not as α- helix but as 3–10 helix, while residues 277–283 were assigned to α-helix PubMed:29215007

Appears in Networks:
Annotations
Confidence
High

complex(a(GO:"filamentous actin"), p(HGNC:MAPT, frag("277_280"))) increases a(HBP:HBP00170) View Subject | View Object

The analysis suggests that the experimental NOE data witness the formation of helical structure in these regions upon binding to F-actin, but the number of detected restraints is not sufficient to define a unique conformation PubMed:29215007

Appears in Networks:
Annotations
Confidence
High

p(HGNC:MAPT, frag("277_280")) increases a(HBP:HBP00170) View Subject | View Object

Analysis of secondary structure in the lowest energy conformation using STRIDE47, identifies α-helix for residues 261–268 and 3–10 helix for residues 277–280 PubMed:29215007

Appears in Networks:
Annotations
Confidence
High

p(HGNC:MAPT, frag("315_318")) increases a(HBP:HBP00170) View Subject | View Object

In most structures a 3–10 helix was identified for residues 315–318, although in the lowest energy structure residues 315–318 are in α-helical conformation (Supplementary Figure 12c) PubMed:29215007

Appears in Networks:
Annotations
Confidence
High

Out-Edges 0

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.