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

The effect of a proline residue on the rate of growth and the space group of alpha-spectrin SH3-domain crystals.

Acta crystallographica. Section D, Biological crystallography - 1 Dec 2009

Cámara-Artigas Ana, Andújar-Sánchez Monserrat, Ortiz-Salmerón Emilia, Cuadri Celia, Casares Salvador

Abstract excerpt

alpha-Spectrin SH3-domain (Spc-SH3) crystallization is characterized by very fast growth of the crystals in the presence of ammonium sulfate as a precipitant agent. The origin of this behaviour can be attributed to the presence of a proline residue that participates in a crystal contact mimicking the binding of proline-rich sequences to SH3 domains. This residue, Pro20, is located in the RT loop and is the main...

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

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Proline

Share to Protein Multimerization

Share to Protein Structure, Quaternary

Share to Spectrin

Share to src Homology Domains

Source

Identifiers

PMID: 19966410
DOI: 10.1107/S0907444909038037

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The effect of a proline residue on the rate of growth and the space group of alpha-spectrin SH3-domain crystals.PMID 19966410Read ↗

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 ↗

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

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

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

Atomic resolution structure of a mutant of the spectrin SH3 domain.Semantic proximity Read ↗

Characterization of oligomers of heterogeneous size as precursors of amyloid fibril nucleation of an SH3 domain: an experimental kinetics study.Semantic proximity Read ↗

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

Role of native topology investigated by multiple unfolding simulations of four SH3 domains.Semantic proximity Read ↗

The SH3-fold family: experimental evidence and prediction of variations in the folding pathways.Semantic proximity Read ↗

Electrostatic effects in the folding of the SH3 domain of the c-Src tyrosine kinase: pH-dependence in 3D-domain swapping and amyloid formation.Semantic proximity Read ↗

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

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