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

Loop movement and catalysis in creatine kinase.

IUBMB life - 1 Jan 2000

Wang Pan-Fen, Flynn Allen J, McLeish Michael J, Kenyon George L

Abstract excerpt

Recently the crystal structure of creatine kinase from Torpedocalifornica was determined to 2.1 A. The dimeric structure revealed two different forms in the unit cell: one monomer was bound to a substrate, MgADP, and the other monomer was bound to a transition-state analogue complex composed of MgADP, nitrate and creatine. The most striking difference between the structures is the movement of two loops...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Diphosphate
Share to Alanine
Share to Aspartic Acid

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

Share to Circular Dichroism

Share to Creatine Kinase

Share to Histidine

Share to Torpedo

Source

Identifiers

PMID: 16036620
DOI: 10.1080/15216540500091999

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

Loop movement and catalysis in creatine kinase.PMID 16036620Read ↗

Structural asymmetry and intersubunit communication in muscle creatine kinase.Semantic proximity Read ↗

Transition state stabilization by six arginines clustered in the active site of creatine kinase.Semantic proximity Read ↗

Roles of amino acid residues H66 and D326 in the creatine kinase activity and structural stability.Semantic proximity Read ↗

Probing binding and occlusion of substrate in the human creatine transporter-1 by computation and mutagenesis.Semantic proximity Read ↗

The role of Arg-96 in Danio rerio creatine kinase in substrate recognition and active center configuration.Semantic proximity Read ↗

Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability.Semantic proximity Read ↗

Mutation of cis-proline 207 in mitochondrial creatine kinase to alanine leads to increased acid stability.Semantic proximity Read ↗

Crystal structure of a cAMP-dependent protein kinase mutant at 1.26A: new insights into the catalytic mechanism.Semantic proximity Read ↗

Investigation of the role of the domain linkers in separate site catalysis by Clostridium symbiosum pyruvate phosphate dikinase.Semantic proximity Read ↗

Creatine kinase isoenzymes specificities: histidine 65 in human CK-BB, a role in protein stability, not in catalysis.Semantic proximity Read ↗

Mutation of the conserved Asp122 in the linker impedes creatine kinase reactivation and refolding.Semantic proximity Read ↗

Identification of substrate contact residues important for the allosteric regulation of phosphofructokinase from Eschericia coli.Semantic proximity Read ↗

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