Troponina C tipo 1
(Redirección desde «TNNC1»)
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| PDB 1aj4 | |
Troponina C 1, músculo esquelético lento e cardíaca
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| Identificadores | |
| Símbolo | TNNC1 ; CMD1Z; CMH13; TN-C; TNC; TNNC |
| Entrez | 7134 |
| OMIM | |
| RefSeq | NP_003271 |
| UniProt | P63316 |
| Outros datos | |
| Locus | Cr. 3 p21.3-14.3.(52.49 – 52.49 Mb) |
A troponina C, músculos esquelético lento e cardíaco ou troponina C tipo 1 (TNNC1) é unha proteína que nos humanos está codificada no xene TNNC1 do cromosoma 3.[1] É unha das dúas isoformas da troponina C; a outra é a TNNC2. Esta isoforma intervén na regulación da contracción muscular no músculo esquelético de contracción lenta e no músculo cardíaco ao unirse a ións calcio. Cando está unida ao calcio, a contracción muscular é posible. A troponina é un complexo de tres subunidades proteicas: troponina C, T e I.
Interaccións
[editar | editar a fonte]A troponina C tipo 1 interacciona con TNNI3.[2][3][4][5][6]
Notas
[editar | editar a fonte]- ↑ "Entrez Gene: TNNC1 troponin C type 1 (slow)".
- ↑ Ward, Douglas G; Brewer Susan M; Gallon Clare E; Gao Yuan; Levine Barry A; Trayer Ian P (May 2004). "NMR and mutagenesis studies on the phosphorylation region of human cardiac troponin I". Biochemistry (United States) 43 (19): 5772–81. ISSN 0006-2960. PMID 15134451. doi:10.1021/bi036310m.
- ↑ Ward, Douglas G; Brewer Susan M; Calvert Melanie J; Gallon Clare E; Gao Yuan; Trayer Ian P (Apr 2004). "Characterization of the interaction between the N-terminal extension of human cardiac troponin I and troponin C". Biochemistry (United States) 43 (13): 4020–7. ISSN 0006-2960. PMID 15049709. doi:10.1021/bi036128l.
- ↑ Ward, Douglas G; Brewer Susan M; Cornes Michael P; Trayer Ian P (Sep 2003). "A cross-linking study of the N-terminal extension of human cardiac troponin I". Biochemistry (United States) 42 (34): 10324–32. ISSN 0006-2960. PMID 12939162. doi:10.1021/bi034495r.
- ↑ Wang, Xu; Li Monica X; Sykes Brian D (Aug 2002). "Structure of the regulatory N-domain of human cardiac troponin C in complex with human cardiac troponin I147-163 and bepridil". J. Biol. Chem. (United States) 277 (34): 31124–33. ISSN 0021-9258. PMID 12060657. doi:10.1074/jbc.M203896200.
- ↑ Li, Monica X; Saude Erik J; Wang Xu; Pearlstone Joyce R; Smillie Lawrence B; Sykes Brian D (Jul 2002). "Kinetic studies of calcium and cardiac troponin I peptide binding to human cardiac troponin C using NMR spectroscopy". Eur. Biophys. J. (Germany) 31 (4): 245–56. ISSN 0175-7571. PMID 12122471. doi:10.1007/s00249-002-0227-1.
Véxase tamén
[editar | editar a fonte]Bibliografía
[editar | editar a fonte]- Gomes AV, Potter JD (2005). "Cellular and molecular aspects of familial hypertrophic cardiomyopathy caused by mutations in the cardiac troponin I gene.". Mol. Cell. Biochem. 263 (1-2): 99–114. PMID 15524171. doi:10.1023/B:MCBI.0000041852.42291.aa.
- Tomasselli AG, Hui JO, Adams L; et al. (1991). "Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus.". J. Biol. Chem. 266 (22): 14548–53. PMID 1907279.
- Schreier T, Kedes L, Gahlmann R (1991). "Cloning, structural analysis, and expression of the human slow twitch skeletal muscle/cardiac troponin C gene.". J. Biol. Chem. 265 (34): 21247–53. PMID 2250022.
- Gahlmann R, Wade R, Gunning P, Kedes L (1988). "Differential expression of slow and fast skeletal muscle troponin C. Slow skeletal muscle troponin C is expressed in human fibroblasts.". J. Mol. Biol. 201 (2): 379–91. PMID 3166492. doi:10.1016/0022-2836(88)90145-3.
- Roher A, Lieska N, Spitz W (1986). "The amino acid sequence of human cardiac troponin-C.". Muscle Nerve 9 (1): 73–7. PMID 3951483. doi:10.1002/mus.880090112.
- Grand RJ, Levine BA, Perry SV (1982). "Proton-magnetic-resonance studies on the interaction of rabbit skeletal-muscle troponin I with troponin C and actin.". Biochem. J. 203 (1): 61–8. PMC 1158193. PMID 7103951.
- Thierfelder L, Watkins H, MacRae C; et al. (1994). "Alpha-tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: a disease of the sarcomere.". Cell 77 (5): 701–12. PMID 8205619. doi:10.1016/0092-8674(94)90054-X.
- Jha PK, Leavis PC, Sarkar S (1997). "Interaction of deletion mutants of troponins I and T: COOH-terminal truncation of troponin T abolishes troponin I binding and reduces Ca2+ sensitivity of the reconstituted regulatory system.". Biochemistry 35 (51): 16573–80. PMID 8987992. doi:10.1021/bi9622433.
- Song WJ, Van Keuren ML, Drabkin HA; et al. (1997). "Assignment of the human slow twitch skeletal muscle/cardiac troponin C gene (TNNC1) to human chromosome 3p21.3-->3p14.3 using somatic cell hybrids.". Cytogenet. Cell Genet. 75 (1): 36–7. PMID 8995486. doi:10.1159/000134453.
- Takeda S, Kobayashi T, Taniguchi H; et al. (1997). "Structural and functional domains of the troponin complex revealed by limited digestion.". Eur. J. Biochem. 246 (3): 611–7. PMID 9219516. doi:10.1111/j.1432-1033.1997.00611.x.
- Spyracopoulos L, Li MX, Sia SK; et al. (1997). "Calcium-induced structural transition in the regulatory domain of human cardiac troponin C.". Biochemistry 36 (40): 12138–46. PMID 9315850. doi:10.1021/bi971223d.
- Keane NE, Quirk PG, Gao Y; et al. (1997). "The ordered phosphorylation of cardiac troponin I by the cAMP-dependent protein kinase--structural consequences and functional implications.". Eur. J. Biochem. 248 (2): 329–37. PMID 9346285. doi:10.1111/j.1432-1033.1997.00329.x.
- Stefancsik R, Jha PK, Sarkar S (1998). "Identification and mutagenesis of a highly conserved domain in troponin T responsible for troponin I binding: potential role for coiled coil interaction.". Proc. Natl. Acad. Sci. U.S.A. 95 (3): 957–62. PMC 18637. PMID 9448267. doi:10.1073/pnas.95.3.957.
- Vassylyev DG, Takeda S, Wakatsuki S; et al. (1998). "Crystal structure of troponin C in complex with troponin I fragment at 2.3-A resolution.". Proc. Natl. Acad. Sci. U.S.A. 95 (9): 4847–52. PMC 20176. PMID 9560191. doi:10.1073/pnas.95.9.4847.
- Redwood C, Lohmann K, Bing W; et al. (2000). "Investigation of a truncated cardiac troponin T that causes familial hypertrophic cardiomyopathy: Ca(2+) regulatory properties of reconstituted thin filaments depend on the ratio of mutant to wild-type protein.". Circ. Res. 86 (11): 1146–52. PMID 10850966. doi:10.1161/01.res.86.11.1146.
- Hoffmann B, Schmidt-Traub H, Perrot A; et al. (2001). "First mutation in cardiac troponin C, L29Q, in a patient with hypertrophic cardiomyopathy.". Hum. Mutat. 17 (6): 524. PMID 11385718. doi:10.1002/humu.1143.
- Schmidtmann A, Lohmann K, Jaquet K (2002). "The interaction of the bisphosphorylated N-terminal arm of cardiac troponin I-A 31P-NMR study.". FEBS Lett. 513 (2-3): 289–93. PMID 11904166. doi:10.1016/S0014-5793(02)02340-2.
- Lindhout DA, Li MX, Schieve D, Sykes BD (2002). "Effects of T142 phosphorylation and mutation R145G on the interaction of the inhibitory region of human cardiac troponin I with the C-domain of human cardiac troponin C.". Biochemistry 41 (23): 7267–74. PMID 12044157. doi:10.1021/bi020100c.
- Wang X, Li MX, Sykes BD (2002). "Structure of the regulatory N-domain of human cardiac troponin C in complex with human cardiac troponin I147-163 and bepridil.". J. Biol. Chem. 277 (34): 31124–33. PMID 12060657. doi:10.1074/jbc.M203896200.
- Li MX, Saude EJ, Wang X; et al. (2003). "Kinetic studies of calcium and cardiac troponin I peptide binding to human cardiac troponin C using NMR spectroscopy.". Eur. Biophys. J. 31 (4): 245–56. PMID 12122471. doi:10.1007/s00249-002-0227-1.
