Difference between revisions of "Part:BBa K4322000"
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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 and chromoproteins, will allow non-covalent crosslinking to occur between chromoprotein csgA fusion nanofibers [2]. The interaction between the knob and hole domain of fibrin-csgA fusion proteins will also allow for increased stability in microbial-ink hydrogel production [2] | + | This documented part, when fused with protein csgA of the curli operon and chromoproteins, will allow non-covalent crosslinking to occur between chromoprotein csgA fusion nanofibers [2]. The interaction between the knob and hole domain of fibrin-csgA fusion proteins will also allow for increased stability in microbial-ink hydrogel production [2] This part contains the fibrin alpha knob domain. |
Latest revision as of 00:49, 4 October 2022
Fibrin Knob Domain (Alpha)
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 and chromoproteins, will allow non-covalent crosslinking to occur between chromoprotein csgA fusion nanofibers [2]. The interaction between the knob and hole domain of fibrin-csgA fusion proteins will also allow for increased stability in microbial-ink hydrogel production [2] This part contains the fibrin alpha knob 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]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]