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

Crystal structure of circular permuted RoCBM21 (CP90): dimerisation and proximity of binding sites.

PloS one - 1 Jan 2012

Stephen Preyesh, Cheng Kuo-Chang, Lyu Ping-Chiang

Abstract excerpt

Glucoamylases, containing starch-binding domains (SBD), have a wide range of scientific and industrial applications. Random mutagenesis and DNA shuffling of the gene encoding a starch-binding domain have resulted in only minor improvements in the affinities of the corresponding protein to their ligands, whereas circular permutation of the RoCBM21 substantially improved its binding affinity and selectivity towards...

Read the complete abstract on PubMed

Topics

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

Share to Amylose
Share to Binding Sites
Share to Crystallography, X-Ray

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

Share to Glucan 1,4-alpha-Glucosidase

Share to Ligands

Share to Mutagenesis, Site-Directed

Share to Protein Multimerization

Share to Protein Structure, Quaternary

Source

Open in PubMed Open full text

Identifiers

PMID: 23226294
DOI: 10.1371/journal.pone.0050488
PMCID: PMC3511584

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

Crystal structure of circular permuted RoCBM21 (CP90): dimerisation and proximity of binding sites.PMID 23226294Read ↗

Glucoamylase: structure/function relationships, and protein engineering.Semantic proximity Read ↗

Tryptophan introduction can change β-glucan binding ability of the carbohydrate-binding module of endo-1,3-β-glucanase.Semantic proximity Read ↗

Carbohydrate binding module recognition of xyloglucan defined by polar contacts with branching xyloses and CH-Π interactions.Semantic proximity Read ↗

Engineering a circularly permuted GFP scaffold for peptide presentation.Semantic proximity Read ↗

Novel xylan-binding properties of an engineered family 4 carbohydrate-binding module.Semantic proximity Read ↗

Small angle X-ray studies reveal that Aspergillus niger glucoamylase has a defined extended conformation and can form dimers in solution.Semantic proximity Read ↗

Engineering the affinity of a family 11 carbohydrate binding module to improve binding of branched over unbranched polysaccharides.Semantic proximity Read ↗

Importance of hydrophobic and polar residues in ligand binding in the family 15 carbohydrate-binding module from Cellvibrio japonicus Xyn10C.Semantic proximity Read ↗

Clostridium thermocellum thermostable lichenase with circular permutations and modifications in the N-terminal region retains its activity and thermostability.Semantic proximity Read ↗

Structural Insight of a Trimodular Halophilic Cellulase with a Family 46 Carbohydrate-Binding Module.Semantic proximity Read ↗

Novel characteristics of a carbohydrate-binding module 20 from hyperthermophilic bacterium.Semantic proximity Read ↗

Family 46 Carbohydrate-binding Modules Contribute to the Enzymatic Hydrolysis of Xyloglucan and β-1,3-1,4-Glucans through Distinct Mechanisms.Semantic proximity Read ↗

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