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

Calmodulin binds to caldesmon in an antiparallel manner.

Biochemistry - 2 Dec 1997

Wang E, Zhuang S, Kordowska J, Grabarek Z, Wang C L

Abstract excerpt

Two of the five tryptophan residues (W659 and W692) in chicken gizzard smooth muscle caldesmon (CaD) are located within the calmodulin (CaM) binding sites in the C-terminal region of the molecule. When these Trp residues are replaced with Gly in either recombinant fragments or synthetic peptides of CaD, the affinity for CaM is decreased by at least 10-fold, suggesting that both of these residues are important for...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Calcium
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Peptide Fragments

Share to Protein Binding

Share to Protein Conformation

Source

Identifiers

PMID: 9398229
DOI: 10.1021/bi963075h

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Calmodulin binds to caldesmon in an antiparallel manner.PMID 9398229Read ↗

Calmodulin binds to Drosophila TRP with an unexpected mode.Semantic proximity Read ↗

Multiple-sited interaction of caldesmon with Ca(2+)-calmodulin.Semantic proximity Read ↗

Interaction of smooth muscle caldesmon with calmodulin mutants.Semantic proximity Read ↗

Calcium binding to calmodulin mutants monitored by domain-specific intrinsic phenylalanine and tyrosine fluorescence.Semantic proximity Read ↗

Spectroscopic characterization of the interaction between calmodulin-dependent protein kinase I and calmodulin.Semantic proximity Read ↗

Characterization of phospho-(tyrosine)-mimetic calmodulin mutants.Semantic proximity Read ↗

Characterisation of tyrosine-phosphorylation-defective calmodulin mutants.Semantic proximity Read ↗

Calcium binding to calmodulin mutants having domain-specific effects on the regulation of ion channels.Semantic proximity Read ↗

Calmodulin mutant in central linker reduces the binding affinity with PreIQ and IQ while interacting with CaV1.2 channels.Semantic proximity Read ↗

Differential binding of calmodulin domains to constitutive and inducible nitric oxide synthase enzymes.Semantic proximity Read ↗

Restoration of the calcium binding activity of mutant calmodulins toward normal by the presence of a calmodulin binding structure.Semantic proximity Read ↗

Fluorescence analysis of calmodulin mutants containing tryptophan: conformational changes induced by calmodulin-binding peptides from myosin light chain kinase and protein kinase II.Semantic proximity Read ↗

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