Abstracts - faqs.org

Abstracts

Zoology and wildlife conservation

Search abstracts:
Abstracts » Zoology and wildlife conservation

Structure-based drug design

Article Abstract:

The information about the three-dimensional structures of macromolecules is a useful basis for the designing of new drugs. The refinement, resolution and the restraints in the structural analysis determine the accuracy of the three-dimensional structures. The structure-based drug designs initially involve the graphical display of hydrogen bonds, molecular surfaces and electrostatic fields. The target protein is defined and the active site that will bind the ligands is computed. The structure-based approach will play a important role in the designing of new proteins, drugs and vaccines.

Author: Blundell, Tom L.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
Usage, Drugs, Structure-activity relationships (Pharmacology), Macromolecules

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site

Article Abstract:

Porphobilinogen deaminase (PBGD), an important enzyme in the biosynthetic pathway of tetrapyrroles, is structurally similar to the transferrins and periplasmic binding proteins. PBGD's dipyrromethane cofactor is covalently associated with domain 3 but is also attached to the salt-bridges and hydrogen-bonds in the cleft separating domains 1 and 2 in a location that corresponds to the binding sites for small-molecule ligands in the protein analogues. This structure, verified by X-ray analysis, indicates that PBGD has one catalytic site.

Author: Louie, Gordon V., Brownlie, Paul D., Lambert, Richard, Cooper, Jonathan B., Blundell, Tom L., Wood, Steve P., Warren, Martin J., Woodcock, Sarah C., Jordan, Peter M.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
Enzymes, Porphobilinogen

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Brief encounters bolster contacts

Article Abstract:

Structural evidence is provided for the transient interactions necessary for the formation of multi-component complexes of proteins, nucleic acids and other molecules. It is shown that rare encounter complexes might control not only the kinetics of the assembly process, but also the way the complex is put together and hence the population of nonspecific complexes can be restricted by the order in which the different subunits are assembled.

Author: Blundell, Tom L., Fernandez-Recio, Juan
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
United Kingdom, Science & research, Biological Product (except Diagnostic) Manufacturing, Drugs, Nucleic Acids, Analysis, Nuclear magnetic resonance spectroscopy, Structure, Chemical properties, Hydrophobic effect, Protein-protein interactions

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: Research
Similar abstracts:
  • Abstracts: Signatures guide drug choice. New exchange, new target. The ins and outs of signalling
  • Abstracts: Hughes looks east for next expansion. Hurricane pounds Florida research facilities. How much green in the greenhouse?
  • Abstracts: Pictures of MHC restriction. The duck's dilemma. Flying the first class flag
  • Abstracts: The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Receptor-associated Mad homologues synergize as effectors of the TGF-beta response
  • Abstracts: Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2025 Advameg, Inc.