Difference between revisions of "Part:BBa K4322001"
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Fibrin is an insoluble protein that is produced in animals in response to bleeding. Fibrin arranges into long fibrous chains that form on the surfaces of activated platelets; together, they produce clots that hinder further blood loss. The polymerization of these long fibrous chains relies on the interaction between N-terminal A- and B-knobs and corresponding a- and b-holes in the γ- and β-modules of fibrin [1]. | Fibrin is an insoluble protein that is produced in animals in response to bleeding. Fibrin arranges into long fibrous chains that form on the surfaces of activated platelets; together, they produce clots that hinder further blood loss. The polymerization of these long fibrous chains relies on the interaction between N-terminal A- and B-knobs and corresponding a- and b-holes in the γ- and β-modules of fibrin [1]. | ||
− | This documented part, when fused with protein csgA of the curli operon | + | This documented part, when fused with protein csgA of the curli operon, will allow non-covalent crosslinking to occur between csgA-α chromoprotein and csgA-γ fusion nanofibers [2]. Additionally, the interaction between the knob and hole domain of fibrin-csgA fusion proteins (i.e csgA-α and csgA-γ) will allow for increased stability in microbial-ink hydrogel production [2]. This part contains the fibrin gamma hole domain. |
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<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
− | <partinfo> | + | <partinfo>BBa_K4322001 SequenceAndFeatures</partinfo> |
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===Functional Parameters=== | ===Functional Parameters=== | ||
− | <partinfo> | + | <partinfo>BBa_K4322001 parameters</partinfo> |
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Latest revision as of 03:29, 4 October 2022
Fibrin Hole Domain (Gamma)
Fibrin is an insoluble protein that is produced in animals in response to bleeding. Fibrin arranges into long fibrous chains that form on the surfaces of activated platelets; together, they produce clots that hinder further blood loss. The polymerization of these long fibrous chains relies on the interaction between N-terminal A- and B-knobs and corresponding a- and b-holes in the γ- and β-modules of fibrin [1].
This documented part, when fused with protein csgA of the curli operon, will allow non-covalent crosslinking to occur between csgA-α chromoprotein and csgA-γ fusion nanofibers [2]. Additionally, the interaction between the knob and hole domain of fibrin-csgA fusion proteins (i.e csgA-α and csgA-γ) will allow for increased stability in microbial-ink hydrogel production [2]. This part contains the fibrin gamma hole domain.
References:
[1]R. I. Litvinov et al., “Polymerization of fibrin: direct observation and quantification of individual B:b knob-hole interactions,” Blood, vol. 109, no. 1, pp. 130–138, Jan. 2007, doi: 10.1182/blood-2006-07-033910.
[2]A. M. Duraj-Thatte et al., “Programmable microbial ink for 3D printing of living materials produced from genetically engineered protein nanofibers,” Nat Commun, vol. 12, no. 1, p. 6600, Dec. 2021, doi: 10.1038/s41467-021-26791-x.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 370
- 1000COMPATIBLE WITH RFC[1000]