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

Deletion of the carboxy terminal part of stefin B does not have a major effect for binding to papain.

Biomedica biochimica acta - 1 Jan 1991

Jerala R, Kroon-Zitko L, Kopitar M, Popovic T, Turk V

Abstract excerpt

Determination of crystal structures of chicken cystatin and human stefin B complexed with papain revealed a novel model of protease inhibition and also structural differences between two cysteine proteinase inhibitor (CPI) families. According to the 3D alignment, stefins have an extension of 9 amino acids on their carboxy terminus in comparison with cystatins. The extension was not expected to make a major...

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 Base Sequence
Share to Binding Sites

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

Share to Chromosome Deletion

Share to Kinetics

Share to Molecular Sequence Data

Share to Mutation

Source

Identifiers

PMID: 1801733

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

Deletion of the carboxy terminal part of stefin B does not have a major effect for binding to papain.PMID 1801733Read ↗

Molecular mechanism of inhibition of cysteine proteinases by their protein inhibitors: kinetic studies with natural and recombinant variants of cystatins and stefins.Semantic proximity Read ↗

Mutations in the QVVAG region of the cysteine proteinase inhibitor stefin B.Semantic proximity Read ↗

Contributions of individual residues in the N-terminal region of cystatin B (stefin B) to inhibition of cysteine proteinases.Semantic proximity Read ↗

Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases.Semantic proximity Read ↗

The role of the second binding loop of the cysteine protease inhibitor, cystatin A (stefin A), in stabilizing complexes with target proteases is exerted predominantly by Leu73.Semantic proximity Read ↗

Production, inhibitory activity, folding and conformational analysis of an N-terminal and an internal deletion variant of chicken cystatin.Semantic proximity Read ↗

Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K+ channel inhibitor-like fold.Semantic proximity Read ↗

Mouse stefins A1 and A2 (Stfa1 and Stfa2) differentiate between papain-like endo- and exopeptidases.Semantic proximity Read ↗

The N-terminal part of recombinant human tear lipocalin/von Ebner's gland protein confers cysteine proteinase inhibition depending on the presence of the entire cystatin-like sequence motifs.Semantic proximity Read ↗

Differences in aggregation properties of three site-specific mutants of recombinant human stefin B.Semantic proximity Read ↗

Essential role of proline isomerization in stefin B tetramer formation.Semantic proximity Read ↗

The Staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease.Semantic proximity Read ↗

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