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Related Concept Videos

Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...

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Updated: Jun 24, 2026

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding
11:07

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding

Published on: September 21, 2011

A proposed consensus steroid-binding sequence--a reply.

S E Fawell1, J A Lees, M G Parker

  • 1Molecular Endocrinology Laboratory, Imperial Cancer Research Fund, Lincoln's Inn Fields, London, United Kingdom.

Molecular Endocrinology (Baltimore, Md.)
|June 1, 1989
PubMed
Summary
This summary is machine-generated.

Researchers investigated a proposed consensus sequence for steroid binding in the mouse estrogen receptor. Findings suggest this motif may not be essential for estradiol binding, challenging its functional significance in steroid receptors.

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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
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Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
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Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
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Area of Science:

  • Molecular biology
  • Endocrinology
  • Protein structure-function relationships

Background:

  • A conserved amino acid sequence motif has been hypothesized as crucial for steroid binding across various steroid-binding proteins.
  • This consensus sequence is based on sequence homology observed in steroidogenic enzymes, steroid-binding proteins, and steroid receptors.

Purpose of the Study:

  • To precisely determine the minimal sequence requirements for steroid binding within the mouse estrogen receptor.
  • To functionally validate the proposed consensus sequence's necessity for estradiol binding.

Main Methods:

  • Utilized deletion mutagenesis to create modified mouse estrogen receptor variants.
  • Employed Scatchard analysis to quantitatively assess the binding affinity of these mutants for estradiol.

Main Results:

  • A specific mutant, lacking the entirety of the proposed consensus sequence, demonstrated undiminished estradiol binding affinity compared to the wild-type receptor.
  • This indicates that the consensus sequence is not strictly required for high-affinity estradiol interaction.

Conclusions:

  • The functional significance of the proposed consensus sequence for steroid binding in the estrogen receptor is questionable.
  • Further research is needed to identify the true determinants of steroid binding specificity and affinity in estrogen receptors.