Difference between revisions of "Part:BBa K5185003"
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The integrin α1 domain (α1) is part of the integrin α1β1 complex, a cell surface receptor involved in cell adhesion, motility, and signal transduction. This domain is responsible for binding to extracellular matrix (ECM) proteins, particularly collagen. By studying and potentially modifying the α1 domain, we can influence cell ECM interactions relevant to tissue engineering and therapeutic interventions. | The integrin α1 domain (α1) is part of the integrin α1β1 complex, a cell surface receptor involved in cell adhesion, motility, and signal transduction. This domain is responsible for binding to extracellular matrix (ECM) proteins, particularly collagen. By studying and potentially modifying the α1 domain, we can influence cell ECM interactions relevant to tissue engineering and therapeutic interventions. | ||
− | + | Other than α1, this part collection includes α2 and CBMs. This part collection of CBMs aimed to provide first aid wound dressings with enhanced antimicrobial functions and a wider and more complex application, where we characterize bacterial cellulose modification methods and constructs using CBMs as a binding domain, linking HNPs such as HNP1 and HNP4 to carbohydrates such as cellulose and chitosan. By incorporating α1 into proteins, collagen-containing materials can be effective targets for modification or degradation. The part collection includes: Cellulose binding matrices CBM2 (<partinfo>BBa_K4011001 </partinfo>) which binds to trehalose, CBM3 (<partinfo>BBa_K4011000</partinfo>) which binds to fibrin, CBM5 (<partinfo>BBa_K5185002</partinfo>) which binds to chitosan, and VbCBMxx (<partinfo>BBa_K5185008</partinfo>) which binds to sodium alginate. Human integrins α1 domain (<partinfo>BBa_K5185003 </partinfo>) and α2 domain (<partinfo>BBa_K5185004</partinfo>), linking functional proteins to collagen. This part collection can help to achieve modification of cellulose membranes using different modification/functionalization proteins. | |
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− | + | Since collagen in itself promotes new skin cell growth, it could be targeted for use in wound dressings that prioritize wound recovery. | |
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+ | ===Usage and Biology=== | ||
+ | In the human body, the integrin α1 domain mediates cell adhesion to collagen types I and IV, playing essential roles in tissue remodeling, wound healing, and angiogenesis. This domain contains a metal-ion-dependent adhesion site (MIDAS) crucial for ligand binding. The α1 domain also participates in intracellular signaling pathways that regulate cell proliferation, differentiation, and survival. The structure of the integrin α1 domain is available in the Protein Data Bank (accession: 1PT6). | ||
+ | Research involving the α1 domain includes exploring its role in treating medical conditions such as fibrosis, cancer, and inflammatory conditions, making it a target for therapeutic development. | ||
− | + | ===Source=== | |
− | === | + | The integrin α1 domain is derived from human cells expressing the integrin α1β1 complex. |
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Revision as of 19:24, 1 October 2024
Human integrins α1 domain(α1)
The integrin α1 domain (α1) is part of the integrin α1β1 complex, a cell surface receptor involved in cell adhesion, motility, and signal transduction. This domain is responsible for binding to extracellular matrix (ECM) proteins, particularly collagen. By studying and potentially modifying the α1 domain, we can influence cell ECM interactions relevant to tissue engineering and therapeutic interventions.
Other than α1, this part collection includes α2 and CBMs. This part collection of CBMs aimed to provide first aid wound dressings with enhanced antimicrobial functions and a wider and more complex application, where we characterize bacterial cellulose modification methods and constructs using CBMs as a binding domain, linking HNPs such as HNP1 and HNP4 to carbohydrates such as cellulose and chitosan. By incorporating α1 into proteins, collagen-containing materials can be effective targets for modification or degradation. The part collection includes: Cellulose binding matrices CBM2 (BBa_K4011001) which binds to trehalose, CBM3 (BBa_K4011000) which binds to fibrin, CBM5 (BBa_K5185002) which binds to chitosan, and VbCBMxx (BBa_K5185008) which binds to sodium alginate. Human integrins α1 domain (BBa_K5185003) and α2 domain (BBa_K5185004), linking functional proteins to collagen. This part collection can help to achieve modification of cellulose membranes using different modification/functionalization proteins.
Since collagen in itself promotes new skin cell growth, it could be targeted for use in wound dressings that prioritize wound recovery.
Usage and Biology
In the human body, the integrin α1 domain mediates cell adhesion to collagen types I and IV, playing essential roles in tissue remodeling, wound healing, and angiogenesis. This domain contains a metal-ion-dependent adhesion site (MIDAS) crucial for ligand binding. The α1 domain also participates in intracellular signaling pathways that regulate cell proliferation, differentiation, and survival. The structure of the integrin α1 domain is available in the Protein Data Bank (accession: 1PT6). Research involving the α1 domain includes exploring its role in treating medical conditions such as fibrosis, cancer, and inflammatory conditions, making it a target for therapeutic development.
Source
The integrin α1 domain is derived from human cells expressing the integrin α1β1 complex.