洞察到Mena的EVH1领域的交互景观

Lanette LaComb1, Agnidipta Ghosh1, Jeffrey B Bonanno1

  • 1Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, United States.

Biochemistry
|August 13, 2024
PubMed
概括

启用/VASP同质性1 (EVH1) 域在疏水裂中结合了富含林的配体. 围绕这些片段的残留物增强了结合亲和力,合成抑制剂的相互作用比天然配体更强.

相关概念视频

Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the...
5.4K
Conservation of Protein Domains02:26

Conservation of Protein Domains

3.1K
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

3.7K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

1.8K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.8K