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相关概念视频

Protein Complex Assembly02:41

Protein Complex Assembly

12.5K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
12.5K
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

2.1K
Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
2.1K
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

2.8K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
2.8K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

4.8K
Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
4.8K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

4.7K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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相关实验视频

Updated: May 1, 2026

Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram
12:21

Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram

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14-3-3zeta的晶体结构:氨酸N-乙转移酶复合体. 脚手架在酶调节中的作用.

T Obsil1, R Ghirlando, D C Klein

  • 1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Cell
|May 5, 2001
PubMed
概括

酶氨酸N-乙转移酶 (AANAT) 调节了氨酸的产生. 它与14-3-3zeta蛋白的相互作用,依赖于酸化,稳定AANAT并调节其活性.

科学领域:

  • 生物化学 生物化学
  • 结构生物学 结构生物学
  • 时间生物学 时间生物学

背景情况:

  • 氨酸N-乙转移酶 (AANAT) 是一种调节氨酸合成的关键酶.
  • AANAT活动对于控制生物过程中的日常节奏至关重要.
  • 已知AANAT与生物组织中的14-3-3蛋白有关.

研究的目的:

  • 为了确定AANAT和14-3-3zeta之间的相互作用的结构基础.
  • 了解这种相互作用如何影响AANAT的酶活性和基质结合.
  • 阐明酸化在调解AANAT-14-3-3zeta复合体形成中的作用.

主要方法:

  • 使用X射线结晶学来确定AANAT-14-3-3zeta复合物的结构.
  • 用热力学测量来评估结合亲和力.
  • 进行了酶活性测定,以量化AANAT功能的调制.

主要成果:

  • 结构显示AANAT结合在14-3-3zeta二次体的中心通道内.
  • 广泛的相互作用稳定了该复合体,涉及14-3-3zeta的光结槽.
  • 通过14-3-3zeta确认了AANAT的酸化依赖的结合.

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Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
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Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram
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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

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  • 这种相互作用通过稳定基质结合区域来调节AANAT活性.
  • 结论:

    • AANAT-14-3-3zeta复合体结构为调节黑激素合成提供了原子洞察力.
    • 14-3-3zeta结合作为一个分子开关,通过结构稳定控制AANAT的酶功能.
    • 了解这种调节机制对于理解昼夜节律控制和潜在的治疗目标至关重要.