molecules-logo

Journal Browser

Journal Browser

Opportunities and Challenges in Protein Crystallography

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Chemical Biology".

Deadline for manuscript submissions: 30 November 2025 | Viewed by 203

Special Issue Editor


E-Mail Website
Guest Editor

Special Issue Information

Dear Colleagues,

Proteins are vital biological macromolecules that play key roles in nearly all aspects of life. The study of protein structure is essential for gaining critical insights in structural biology and related fields, such as structure-based drug discovery and design. Consequently, understanding protein structure holds great practical and fundamental significance, serving as a cornerstone for elucidating the mechanisms underlying various biological processes. In addition, biological macromolecules can inspire researchers to build artificial biomimetic molecular machines to be used to for the most diverse applications, even those not strictly related to biology. In this context, the possibility to acquire structural knowledge, both of an experimental and computational nature, is of paramount importance for optimizing design to improve efficiency. On the other hand, the advent of new computational tools based on artificial intelligence has recently boosted the field of protein crystallography, offering new routes to improve experimental and computational procedures to acquire structural information from experimental data.

This Special Issue seeks to showcase innovative methods for protein crystallization, advancements in diffraction techniques, and the integration of computational modeling with crystallographic methods for structure determination. This Special Issue will also highlight the ongoing challenges in obtaining high-quality crystals and interpreting complex structures. Importantly, we hope to receive contributions from experts reflecting on the future of protein crystallography, emphasizing its role in drug discovery, biocatalysis, and synthetic biology.

We invite the submission of contributions that elucidate the significance of protein crystallography in both fundamental research and applied sciences, setting the stage for future breakthroughs in understanding biological processes at the molecular level.

We look forward to receiving your contributions.

You may choose our Joint Special Issue in Solids.

Dr. Rocco Caliandro
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • protein crystals
  • X-ray diffraction
  • cryo-EM
  • small-angle X-ray scattering
  • phasing methods
  • structural analysis

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • Reprint: MDPI Books provides the opportunity to republish successful Special Issues in book format, both online and in print.

Further information on MDPI's Special Issue policies can be found here.

Published Papers (1 paper)

Order results
Result details
Select all
Export citation of selected articles as:

Research

13 pages, 3078 KB  
Article
A Unique Trimeric Assembly of Human Dishevelled 1 PDZ Domain in Crystal: Implication of Homo- and Hetero-Oligomerization During Wnt Signaling Process
by Shotaro Yasukochi, Nobutaka Numoto, Kiminori Hori, Takeshi Tenno, Emi Hibino, Nobutoshi Ito and Hidekazu Hiroaki
Molecules 2025, 30(17), 3538; https://doi.org/10.3390/molecules30173538 - 29 Aug 2025
Abstract
Wnt/β-catenin signaling is hyper-activated in several cancer cells and cancer stem cells. Dishevelled/Dvl is a key adapter protein that acts as a bridge between the Wnt receptor Frizzled (Fzd) and other cytosolic factors. In detail, the C-terminal cytosolic region is the ligand of [...] Read more.
Wnt/β-catenin signaling is hyper-activated in several cancer cells and cancer stem cells. Dishevelled/Dvl is a key adapter protein that acts as a bridge between the Wnt receptor Frizzled (Fzd) and other cytosolic factors. In detail, the C-terminal cytosolic region is the ligand of the PSD-95, disks large, and zonula occludens-1 (PDZ) domain of Dvl. Therefore, the PDZ domain (Dvl-PDZ) is thought to be a potential drug target. In this paper, we determined the first crystal structure of the PDZ domain of human Dvl1 (hDvl1-PDZ) at a 2.4 Å resolution. The domain was adapted into a unique trimeric form in which all the canonical ligand-binding clefts were occupied by the β2-β3 loop of the neighbor molecule, like an auto-inhibiting trimer. We used solution nuclear magnetic resonance (NMR) experiments to assess the presence of the self-associated oligomer of hDvl1-PDZ in the solution. Introducing the Ala substitution at Asp 272, the key residue of the β2-β3 loop, partly abolished the concentration-dependent chemical shift change, which suggests that this residue is one of the key residues for formation. Based on these observations, we propose an auto-inhibiting trimer formation of Dvl-PDZ in a Dvl-Axin hetero-oligomerization model of Wnt/β-catenin signal transduction. Full article
(This article belongs to the Special Issue Opportunities and Challenges in Protein Crystallography)
Show Figures

Graphical abstract

Back to TopTop