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相关概念视频

Fibril-associated Collagen01:11

Fibril-associated Collagen

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Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
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Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

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Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
Connective tissue proper includes loose...
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Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

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Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can...
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Structural Protein Function01:56

Structural Protein Function

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
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Role of Matrix Metalloproteases in Degradation of ECM01:23

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Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult...
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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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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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对原蛋白中Y-G键的Vibrio原酶VhaC的机理洞察

Wen-Xiao Zhao1,2, Rui Liu1,2, Dan-Dan Wang1,2

  • 1State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China.

Journal of agricultural and food chemistry
|August 22, 2025
PubMed
概括

像VhaC这样的M9原酶在Y-G键上分离原体. 在VhaC中保存的氨酸 (Y549)

关键词:
M9家族分裂地点原蛋白原酶的使用结构基础基质的特异性毒性因子

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Engineering Fibrin-based Tissue Constructs from Myofibroblasts and Application of Constraints and Strain to Induce Cell and Collagen Reorganization
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科学领域:

  • 生物化学
  • 分子生物学
  • 酵素学

背景情况:

  • M9原酶具有高活性和对原的特异性,可用于生物技术和医学.
  • 已知M9原酶的原溶解机制,但它们分裂部位特异性的分子基础尚未完全理解.

研究的目的:

  • 阐明 M9 原酶 VhaC 的 Y-G 键裂解位点特异性的分子机制.
  • 确定负责VhaC基质识别的结构决定因素,特别是在P1'位置.

主要方法:

  • 对M9原酶VhaC的结构分析.
  • 在基质结合中涉及的关键氨基酸残留物的鉴定.
  • 在M9原酶中对保存残留物的比较分析.

主要成果:

  • VhaC的双G图案 (G441和G442) 和Y549形成了一个狭窄的S1'基质结合口袋.
  • 由于其庞大的侧链,Y549作为特定P1'甘氨酸识别的主要决定因素,限制其他残留物.
  • 与Y549相对应的S1'氨酸在M9原酶中保存,表明其功能重要性.

结论:

  • 由S1'结合口的结构约束,特别是Y549的作用决定了VhaC的特定Y-G结合裂变.
  • 了解这种特异性增强了M9原酶在疾病治疗和原寡生产中的潜在应用.