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

Structure-function relationship of serine protease-protein inhibitor interaction.

Acta biochimica Polonica - 1 Jan 2001

Otlewski J, Jaskólski M, Buczek O, Cierpicki T, Czapińska H, Krowarsch D, Smalas A O, Stachowiak D, Szpineta A, Dadlez M

Abstract excerpt

We report our progress in understanding the structure-function relationship of the interaction between protein inhibitors and several serine proteases. Recently, we have determined high resolution solution structures of two inhibitors Apis mellifera chymotrypsin inhibitor-1 (AMCI-I) and Linum usitatissimum trypsin inhibitor (LUTI) in the free state and an ultra high resolution X-ray structure of BPTI. All three...

Read the complete abstract on PubMed

Topics

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

Share to Aprotinin
Share to Bees
Share to Blood Proteins

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

Share to Insect Proteins

Share to Serine Endopeptidases

Share to Serine Proteinase Inhibitors

Share to Thermodynamics

Source

Identifiers

PMID: 11732612

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

Structure-function relationship of serine protease-protein inhibitor interaction.PMID 11732612Read ↗

Single mutation at P1 of a chymotrypsin inhibitor changes it to a trypsin inhibitor: X-ray structural (2.15 A) and biochemical basis.Semantic proximity Read ↗

Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants.Semantic proximity Read ↗

The crystal structures of the complexes between bovine beta-trypsin and ten P1 variants of BPTI.Semantic proximity Read ↗

Substitutions at the P(1) position in BPTI strongly affect the association energy with serine proteinases.Semantic proximity Read ↗

Role of remote scaffolding residues in the inhibitory loop pre-organization, flexibility, rigidification and enzyme inhibition of serine protease inhibitors.Semantic proximity Read ↗

Complexation of two proteic insect inhibitors to the active site of chymotrypsin suggests decoupled roles for binding and selectivity.Semantic proximity Read ↗

Trypsin complexed with alpha 1-proteinase inhibitor has an increased structural flexibility.Semantic proximity Read ↗

High-resolution structure of bovine pancreatic trypsin inhibitor with altered binding loop sequence.Semantic proximity Read ↗

Assessment of the protein interaction between coagulation factor XII and corn trypsin inhibitor by molecular docking and biochemical validation.Semantic proximity Read ↗

X-ray structures of free and leupeptin-complexed human alphaI-tryptase mutants: indication for an alpha-->beta-tryptase transition.Semantic proximity Read ↗

Understanding the molecular basis of stability in Kunitz (STI) family of inhibitors in terms of a conserved core tryptophan residue: A theoretical investigation.Semantic proximity Read ↗

Binding of amino acid side chains to preformed cavities: interaction of serine proteinases with turkey ovomucoid third domains with coded and noncoded P1 residues.Semantic proximity Read ↗

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