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

Identification and characterization of the ATP-binding site in human pancreatic glucokinase.

Archives of biochemistry and biophysics - 1 Apr 2005

Marotta Diane E, Anand Gulshan R, Anderson Timothy A, Miller Stephen P, Okar David A, Levitt David G, Lange Alex J

Abstract excerpt

The central role of human pancreatic glucokinase in insulin secretion and, consequently, in maintenance of blood glucose levels has prompted investigation into identification of ATP-binding site residues and examination of ATP- and glucose-binding interactions. Because glucokinase has been resistant to crystallization, computer generated homology models were developed based on the X-ray crystal structure of the...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Computer Simulation

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

Share to Crystallography, X-Ray

Share to Glucokinase

Share to Glucose

Share to Glucose-6-Phosphate

Share to Pancreas

Share to Substrate Specificity

Source

Identifiers

PMID: 15752705
DOI: 10.1016/j.abb.2005.01.018

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

Identification and characterization of the ATP-binding site in human pancreatic glucokinase.PMID 15752705Read ↗

Structural model of human glucokinase in complex with glucose and ATP: implications for the mutants that cause hypo- and hyperglycemia.Semantic proximity Read ↗

Crystal structure of E339K mutated human glucokinase reveals changes in the ATP binding site.Semantic proximity Read ↗

Identification of a phosphate regulatory site and a low affinity binding site for glucose 6-phosphate in the N-terminal half of human brain hexokinase.Semantic proximity Read ↗

ATP-binding site of human brain hexokinase as studied by molecular modeling and site-directed mutagenesis.Semantic proximity Read ↗

Binding of ATP at the active site of human pancreatic glucokinase--nucleotide-induced conformational changes with possible implications for its kinetic cooperativity.Semantic proximity Read ↗

Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus.Semantic proximity Read ↗

Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants.Semantic proximity Read ↗

Characterization of glucokinase mutations associated with maturity-onset diabetes of the young type 2 (MODY-2): different glucokinase defects lead to a common phenotype.Semantic proximity Read ↗

Study of the regulatory properties of glucokinase by site-directed mutagenesis: conversion of glucokinase to an enzyme with high affinity for glucose.Semantic proximity Read ↗

Regulation of pancreatic beta-cell glucokinase: from basics to therapeutics.Semantic proximity Read ↗

Mutants of glucokinase cause hypoglycaemia- and hyperglycaemia syndromes and their analysis illuminates fundamental quantitative concepts of glucose homeostasis.Semantic proximity Read ↗

Structure-function analysis of the alpha5 and the alpha13 helices of human glucokinase: description of two novel activating mutations.Semantic proximity Read ↗

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