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

Probing the primary structural determinants of streptokinase inter-domain linkers by site-specific substitution and deletion mutagenesis.

Biochimica et biophysica acta - 1 Sept 2010

Yadav Suman, Sahni Girish

Abstract excerpt

The bacterial protein streptokinase (SK) contains three independently folded domains (alpha, beta and gamma), interconnected by two flexible linkers with noticeable sequence homology. To investigate their primary structure requirements, the linkers were swapped amongst themselves i.e. linker 1 (between alpha and beta domains) was swapped with linker 2 (between beta and gamma domains) and vice versa. The resultant...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Hydrolysis
Share to Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Peptide Fragments

Share to Plasminogen

Share to Protein Conformation

Share to Protein Interaction Domains and Motifs

Share to Surface Plasmon Resonance

Source

Identifiers

PMID: 20417732
DOI: 10.1016/j.bbapap.2010.04.003

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Probing the primary structural determinants of streptokinase inter-domain linkers by site-specific substitution and deletion mutagenesis.PMID 20417732Read ↗

Mutation of lysines in a plasminogen binding region of streptokinase identifies residues important for generating a functional activator complex.Semantic proximity Read ↗

Role of the streptokinase alpha-domain in the interactions of streptokinase with plasminogen and plasmin.Semantic proximity Read ↗

Structural and functional basis of plasminogen activation by staphylokinase.Semantic proximity Read ↗

Identification of a new exosite involved in catalytic turnover by the streptokinase-plasmin activator complex during human plasminogen activation.Semantic proximity Read ↗

Functional differences between Streptococcus pyogenes cluster 1 and cluster 2b streptokinases are determined by their β-domains.Semantic proximity Read ↗

Plasminogen substrate recognition by the streptokinase-plasminogen catalytic complex is facilitated by Arg253, Lys256, and Lys257 in the streptokinase beta-domain and kringle 5 of the substrate.Semantic proximity Read ↗

Understanding the role of domain–domain linkers in the spatial orientation of domains in multi-domain proteinsSemantic proximity Read ↗

Computational simulations assessment of mutations impact on streptokinase (SK) from a group G streptococci with enhanced activity - insights into the functional roles of structural dynamics flexibility of SK and stabilization of SK-μplasmin catalytic complex.Semantic proximity Read ↗

The Extracytoplasmic Linker Peptide of the Sensor Protein SaeS Tunes the Kinase Activity Required for Staphylococcal Virulence in Response to Host SignalsSemantic proximity Read ↗

Staphylokinase Requires NH2-terminal Proteolysis for Plasminogen ActivationSemantic proximity Read ↗

The streptokinase gene: allelic variation, genomic environment and expression control.Semantic proximity Read ↗

Structure-function analysis of the streptokinase amino terminus (residues 1-59).Semantic proximity Read ↗

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