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

High-resolution structure of calcium-loaded calbindin D9k.

Journal of molecular biology - 5 Jun 1993

Kördel J, Skelton N J, Akke M, Chazin W J

Abstract excerpt

The three-dimensional solution structure of calcium-loaded calbindin D9k has been determined using experimental constraints obtained from nuclear magnetic resonance spectroscopy. A total of 1176 constraints (16 per residue overall, 32 per residue for the core residues) was used for the final refinement, including 1002 distance and 174 dihedral angle constraints. In addition, 23 hydrogen bond constraints were used...

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Cattle
Share to Computer Simulation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Magnetic Resonance Spectroscopy

Share to Models, Molecular

Share to Mutation

Share to X-Ray Diffraction

Source

Identifiers

PMID: 8515447
DOI: 10.1006/jmbi.1993.1322

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

High-resolution structure of calcium-loaded calbindin D9k.PMID 8515447Read ↗

Characterization of the N-terminal half-saturated state of calbindin D9k: NMR studies of the N56A mutant.Semantic proximity Read ↗

Disulfide bonds in homo- and heterodimers of EF-hand subdomains of calbindin D9k: stability, calcium binding, and NMR studies.Semantic proximity Read ↗

Sequence and context dependence of EF-hand loop dynamics. An 15N relaxation study of a calcium-binding site mutant of calbindin D9k.Semantic proximity Read ↗

The EF-hand domain: a globally cooperative structural unit.Semantic proximity Read ↗

A calbindin D9k mutant with reduced calcium affinity and enhanced cooperativity. Metal ion binding, stability, and structural studies.Semantic proximity Read ↗

Functional properties of calbindin D9K mutants with exchanged Ca2+ binding sites.Semantic proximity Read ↗

Probing fragment complementation by rigid-body docking: in silico reconstitution of calbindin D9k.Semantic proximity Read ↗

Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant.Semantic proximity Read ↗

Design and synthesis of the pseudo-EF hand in calbindin D9K: effect of amino acid substitutions in the alpha-helical regions.Semantic proximity Read ↗

Solvation energetics and conformational change in EF-hand proteins.Semantic proximity Read ↗

Ca2+ binding in proteins of the calmodulin superfamily: cooperativity, electrostatic contributions and molecular mechanisms.Semantic proximity Read ↗

Side chain mobility in bovine calbindin D9k. Rotational motion of Tyr13.Semantic proximity Read ↗

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