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

An extended hydrophobic core induces EF-hand swapping.

Protein science : a publication of the Protein Society - 1 May 2001

Håkansson M, Svensson A, Fast J, Linse S

Abstract excerpt

The structure of calbindin D(9k) with two substitutions was determined by X-ray crystallography at 1.8-A resolution. Unlike wild-type calbindin D(9k), which is a monomeric protein with two EF-hands, the structure of the mutated calbindin D(9k) reveals an intertwined dimer. In the dimer, two EF-hands of the monomers have exchanged places, and thus a 3D domain-swapped dimer has been formed. EF-hand I of molecule A...

Read the complete abstract on PubMed

Topics

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

Share to Amyloidosis
Share to Apoproteins
Share to Calbindins

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

Share to Chromatography, Gel

Share to EF Hand Motifs

Share to Methionine

Share to Protein Structure, Quaternary

Share to S100 Calcium Binding Protein G

Source

Open in PubMed Open full text

Identifiers

PMID: 11316872
DOI: 10.1110/ps.47501
PMCID: PMC2374197

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

An extended hydrophobic core induces EF-hand swapping.PMID 11316872Read ↗

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

Thermodynamic Control of Domain Swapping by Modulating the Helical Propensity in the Hinge Region of Myoglobin.Semantic proximity Read ↗

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

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

Quantitative measurements of the cooperativity in an EF-hand protein with sequential calcium binding.Semantic proximity Read ↗

Symmetrical stabilization of bound Ca2+ ions in a cooperative pair of EF-hands through hydrogen bonding of coordinating water molecules in calbindin D(9k).Semantic proximity Read ↗

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

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

A proposed structural model for amyloid fibril elongation: domain swapping forms an interdigitating beta-structure polymer.Semantic proximity Read ↗

Structure of the monomeric 8-kDa dynein light chain and mechanism of the domain-swapped dimer assembly.Semantic proximity Read ↗

Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions.Semantic proximity Read ↗

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