Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The structure of murine neuroglobin: Novel pathways for ligand migration and binding.

Proteins - 1 Jul 2004

Vallone Beatrice, Nienhaus Karin, Brunori Maurizio, Nienhaus G Ulrich

Abstract excerpt

Neuroglobin, a recently discovered globin predominantly expressed in neuronal tissue of vertebrates, binds small, gaseous ligands at the sixth coordination position of the heme iron. In the absence of an exogenous ligand, the distal histidine (His64) binds to the heme iron in the ferrous and ferric states. The crystal structure of murine ferric (met) neuroglobin at 1.5 A reveals interesting features relevant to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Crystallography, X-Ray
Share to Globins
Share to Heme

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to Ligands

Share to Pliability

Share to Protein Structure, Secondary

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 15162488
DOI: 10.1002/prot.20113

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The structure of murine neuroglobin: Novel pathways for ligand migration and binding.PMID 15162488Read ↗

Engineering the internal cavity of neuroglobin demonstrates the role of the haem-sliding mechanism.Semantic proximity Read ↗

Distal mutation modulates the heme sliding in mouse neuroglobin investigated by molecular dynamics simulation.Semantic proximity Read ↗

Residues in the distal heme pocket of neuroglobin. Implications for the multiple ligand binding steps.Semantic proximity Read ↗

Structural dynamics in the active site of murine neuroglobin and its effects on ligand binding.Semantic proximity Read ↗

Mapping Hydrophobic Tunnels and Cavities in Neuroglobin with Noble Gas under Pressure.Semantic proximity Read ↗

Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin.Semantic proximity Read ↗

A distal ligand mutes the interaction of hydrogen sulfide with human neuroglobin.Semantic proximity Read ↗

Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography.Semantic proximity Read ↗

Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance.Semantic proximity Read ↗

Human neuroglobin and H64A distal variant: How mutation and pH affect the heme pocket.Semantic proximity Read ↗

Nitrosyl Myoglobins and Their Nitrite Precursors: Crystal Structural and Quantum Mechanics and Molecular Mechanics Theoretical Investigations of Preferred Fe -NO Ligand Orientations in Myoglobin Distal Pockets.Semantic proximity Read ↗

Structural characterization of the proximal and distal histidine environment of cytoglobin and neuroglobin.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.