scholarly journals History of Progress and Challenges in Structural Biology

2012 ◽  
Vol s4 ◽  
Author(s):  
Sompop Bencharit
Keyword(s):  
Structural Biology ◽  
History Of

scholarly journals Discovery, development and application of drugs targeting BCL-2 pro-survival proteins in cancer

2021 ◽  
Author(s):  
Erinna F. Lee ◽  
W. Douglas Fairlie
Keyword(s):  
Structural Biology ◽  
Protein Interactions ◽  
Basic Science ◽  
Great Success ◽  
Protein Protein Interactions ◽  
New Class ◽  
Success Stories ◽  
History Of ◽  
Approved Drugs ◽  
Close Relatives

The discovery of a new class of small molecule compounds that target the BCL-2 family of anti-apoptotic proteins is one of the great success stories of basic science leading to translational outcomes in the last 30 years. The eponymous BCL-2 protein was identified over 30 years ago due to its association with cancer. However, it was the unveiling of the biochemistry and structural biology behind it and its close relatives’ mechanism(s)-of-action that provided the inspiration for what are now known as ‘BH3-mimetics’, the first clinically approved drugs designed to specifically inhibit protein–protein interactions. Herein, we chart the history of how these drugs were discovered, their evolution and application in cancer treatment.

scholarly journals The data universe of structural biology

IUCrJ ◽  
2020 ◽  
Vol 7 (4) ◽  
pp. 630-638 ◽  
Author(s):  
Helen M. Berman ◽  
Brinda Vallat ◽  
Catherine L. Lawson
Keyword(s):  
Protein Data Bank ◽  
Structural Biology ◽  
Data Bank ◽  
Small Data ◽  
Complex Structures ◽  
Data Resource ◽  
History Of

The Protein Data Bank (PDB) has grown from a small data resource for crystallographers to a worldwide resource serving structural biology. The history of the growth of the PDB and the role that the community has played in developing standards and policies are described. This article also illustrates how other biophysics communities are collaborating with the worldwide PDB to create a network of interoperating data resources. This network will expand the capabilities of structural biology and enable the determination and archiving of increasingly complex structures.

1. The roots of biochemistry

2021 ◽  
pp. 1-23
Author(s):  
Mark Lorch
Keyword(s):  
Nucleic Acids ◽  
20Th Century ◽  
19Th Century ◽  
Structural Biology ◽  
Ribonucleic Acid ◽  
Alcoholic Beverages ◽  
X Ray ◽  
X Ray Crystallography ◽  
History Of ◽  
The 19Th Century

This chapter traces the history of biochemistry, which is linked to the understanding of arguably the oldest uses of biotechnology—fermentation and the production of alcoholic beverages and cheese. In the 19th century, at the same time as the fermentation debates and enzymology flourished, the nature of proteins was under scrutiny. The chapter then considers the contribution that X-ray crystallography has made to structural biology. By the mid-20th century, the structures of the two massive molecular players, protein and nucleic acids (DNA along with ribonucleic acid), and their myriad roles were in place. It was becoming apparent that these were the fundamental molecular machines that marshal the chemistry within cells.

scholarly journals The history of the PDB as a public resource for enabling science

2014 ◽  
Vol 70 (a1) ◽  
pp. C934-C934
Author(s):  
Helen Berman
Keyword(s):  
Protein Data Bank ◽  
Structural Biology ◽  
Scientific Community ◽  
Access Point ◽  
Data Bank ◽  
Biological Macromolecules ◽  
Science Technology ◽  
Public Resource ◽  
History Of ◽  
Online Access

As the crystal structures of biological macromolecules were being determined, a new field of structural biology was born. Inspired by these new structures, the scientific community worked to establish a home to archive and share the data emerging from these experiments. The Protein Data Bank (PDB) was established in 1971 with seven structures. The PDB provides a repository for scientists who generate the data, and an access point for researchers and students to find the information needed to drive additional studies. Today, the PDB contains and supports online access to ~100,000 biomacromolecules that help researchers understand aspects of biology, including medicine, agriculture, and biological energy. The ways in which the interrelationships among science, technology, and community have driven the evolution of the PDB resource for more than forty years will be discussed. The PDB archive is managed by the Worldwide Protein Data Bank (wwpdb.org), whose members are the RCSB PDB, PDBe, PDBj and BMRB.

scholarly journals The globins: classic structures and new insights

2012 ◽  
Vol 34 (5) ◽  
pp. 52-53
Author(s):  
Clare Sansom
Keyword(s):  
Molecular Biology ◽  
Structural Biology ◽  
Nobel Prize ◽  
Binding Proteins ◽  
Protein Structures ◽  
Dna Structure ◽  
Molecular Medicine ◽  
Oxygen Binding ◽  
Low Resolution ◽  
History Of

The oxygen-binding proteins myoglobin and haemoglobin have a special place in the history of structural biology, and, by implication, of molecular biology and molecular medicine. When the first structures of these proteins were published, in 19581 and 19602, they were the only protein structures known. And even these structures bore very little resemblance to what we now think of as ‘protein structures’. The structures were far too crude – low resolution, as structural biologists say – to reveal the positions of any of the atoms. The beautiful and meticulous hand-drawn diagrams of the myoglobin monomer and the haemoglobin tetramer in these proteins show fat sausage-like shapes representing the eight -helices of the now well-known globin fold, with the haem group nestling in between. It took the genius of the principal scientists involved in that work, Max Perutz and John Kendrew, to imagine the potential of these rather unpromising looking structures. Perutz and Kendrew were jointly awarded the Nobel Prize for Chemistry in 1962, which was a particularly good year for structural biology; Watson, Crick and Wilkins were awarded the Physiology or Medicine Nobel for the DNA structure then too.

scholarly journals Structural Biology Illuminates Molecular Determinants of Broad Ebolavirus Neutralization by Human Antibodies for Pan-Ebolavirus Therapeutic Development

2022 ◽  
Vol 12 ◽  
Author(s):  
Charles D. Murin ◽  
Pavlo Gilchuk ◽  
James E. Crowe ◽  
Andrew B. Ward
Keyword(s):  
Structural Biology ◽  
Severe Disease ◽  
Single Species ◽  
Major Advance ◽  
Additional Species ◽  
Fda Approval ◽  
Molecular Determinants ◽  
Therapeutic Development ◽  
History Of ◽  
Zaire Ebolavirus

Monoclonal antibodies (mAbs) have proven effective for the treatment of ebolavirus infection in humans, with two mAb-based drugs Inmazeb™ and Ebanga™ receiving FDA approval in 2020. While these drugs represent a major advance in the field of filoviral therapeutics, they are composed of antibodies with single-species specificity for Zaire ebolavirus. The Ebolavirus genus includes five additional species, two of which, Bundibugyo ebolavirus and Sudan ebolavirus, have caused severe disease and significant outbreaks in the past. There are several recently identified broadly neutralizing ebolavirus antibodies, including some in the clinical development pipeline, that have demonstrated broad protection in preclinical studies. In this review, we describe how structural biology has illuminated the molecular basis of broad ebolavirus neutralization, including details of common antigenic sites of vulnerability on the glycoprotein surface. We begin with a discussion outlining the history of monoclonal antibody therapeutics for ebolaviruses, with an emphasis on how structural biology has contributed to these efforts. Next, we highlight key structural studies that have advanced our understanding of ebolavirus glycoprotein structures and mechanisms of antibody-mediated neutralization. Finally, we offer examples of how structural biology has contributed to advances in anti-viral medicines and discuss what opportunities the future holds, including rationally designed next-generation therapeutics with increased potency, breadth, and specificity against ebolaviruses.

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