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The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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Aromatic Hydrocarbon Anions: Structural Overview01:18

Aromatic Hydrocarbon Anions: Structural Overview

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Neutral hydrocarbons like cyclopentadiene with an odd number of carbon atoms and one intervening CH2 group in the ring are not aromatic. Cyclopentadiene with 4 π electrons does not satisfy the 4n + 2 π electron rule. Additionally, the intervening CH2 group is sp3 hybridized and lacks a vacant p orbital, thereby interrupting the overlap of p orbitals in a continuous manner and preventing the delocalization of π electrons throughout the ring.
Due to the absence of continuous...
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Ligand Binding Sites02:40

Ligand Binding Sites

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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...
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Conserved Binding Sites01:49

Conserved Binding Sites

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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...
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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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...
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Dissipative Microgravimetry to Study the Binding Dynamics of the Phospholipid Binding Protein Annexin A2 to Solid-supported Lipid Bilayers Using a Quartz Resonator
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Human SEIPIN Binds Anionic Phospholipids.

Renhong Yan1, Hongwu Qian1, Ivan Lukmantara2

  • 1Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, State Key Laboratory of Membrane Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China.

Developmental Cell
|October 9, 2018
PubMed
Summary
This summary is machine-generated.

SEIPIN protein is crucial for fat storage and adipocyte development. Its structure reveals an undecamer formation essential for function, binding phospholipids to maintain ER homeostasis.

Keywords:
BSCL2GPATPI(3)PSEIPINadipogenesisadipose tissuecongenital generalize lipodystrophylipid dropletsphosphatidic acidundecamer

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • Lipid droplet (LD) biogenesis and adipocyte development are key to mammalian fat storage.
  • SEIPIN, an endoplasmic reticulum (ER) integral membrane protein, is vital for both LD formation and adipogenesis.
  • The precise molecular function of SEIPIN remains largely unknown.

Purpose of the Study:

  • To elucidate the molecular function of SEIPIN by determining its structure.
  • To investigate the structural basis for SEIPIN's role in lipid droplet biogenesis and adipogenesis.

Main Methods:

  • Cryogenic electron microscopy (cryo-EM) was used to determine the structure of human SEIPIN.
  • Biochemical assays were performed to assess the binding properties of SEIPIN and its domains.

Main Results:

  • The high-resolution cryo-EM structure of human SEIPIN was determined at 3.8 Å resolution.
  • SEIPIN forms a stable undecamer, an oligomerization state critical for its physiological function.
  • The lumenal domain of SEIPIN exhibits an eight-stranded β sandwich fold and binds anionic phospholipids, including phosphatidic acid.

Conclusions:

  • SEIPIN functions as a scaffold, potentially maintaining phospholipid homeostasis and ER surface tension.
  • The undecameric structure and phospholipid-binding capability of SEIPIN are key to its role in fat storage and adipocyte development.