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

Atomic resolution structure of a mutant of the spectrin SH3 domain.

Acta crystallographica. Section D, Biological crystallography - 1 Feb 2001

Berisio R, Viguera A, Serrano L, Wilmanns M

Abstract excerpt

The crystal structure of an alpha-spectrin Src-homology 3 (SH3) domain mutant has been refined at 1.12 A resolution. This X-ray structure is at the highest resolution achieved so far for an SH3 domain. The structure allows the identification of a complete set of specific interactions and is useful for the elucidation of relations between structure and pH-dependent thermodynamic stability in a series of SH3 domain...

Read the complete abstract on PubMed

Topics

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

Share to Crystallization
Share to Crystallography, X-Ray
Share to Hydrogen Bonding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Protein Structure, Secondary

Share to Sensitivity and Specificity

Share to Spectrin

Share to src Homology Domains

Source

Identifiers

PMID: 11173498
DOI: 10.1107/s090744490001581x

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

Atomic resolution structure of a mutant of the spectrin SH3 domain.PMID 11173498Read ↗

High-resolution structure of an alpha-spectrin SH3-domain mutant with a redesigned hydrophobic core.Semantic proximity Read ↗

Crystal structure of the SH3 domain in human Fyn; comparison of the three‐dimensional structures of SH3 domains in tyrosine kinases and spectrin.Semantic proximity Read ↗

The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved.Semantic proximity Read ↗

Understanding the polymorphic behaviour of a mutant of the α-spectrin SH3 domain by means of two 1.1 Å resolution structures.Semantic proximity Read ↗

Insights into the origin of the tendency of the PI3-SH3 domain to form amyloid fibrils.Semantic proximity Read ↗

A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state.Semantic proximity Read ↗

Structural and thermodynamic studies of Bergerac-SH3 chimeras.Semantic proximity Read ↗

Conformational strain in the hydrophobic core and its implications for protein folding and design.Semantic proximity Read ↗

Hydrogen-exchange stability analysis of Bergerac-Src homology 3 variants allows the characterization of a folding intermediate in equilibrium.Semantic proximity Read ↗

Computer-assisted re-design of spectrin SH3 residue clusters.Semantic proximity Read ↗

A single mutation induces amyloid aggregation in the alpha-spectrin SH3 domain: analysis of the early stages of fibril formation.Semantic proximity Read ↗

Analysis of the thermodynamics of binding of an SH3 domain to proline-rich peptides using a chimeric fusion protein.Semantic proximity Read ↗

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