| SANT domain | |
|---|---|
| Identifiers | |
| Symbol | SANT |
| InterPro | IPR017884 |
| PROSITE | PS51293 |
| CATH | 1fex |
| SCOP2 | 1fex / SCOPe / SUPFAM |
In molecular biology, a SANT domain is a protein domain that allows many chromatin remodeling proteins to interact with histones. [1] The name SANT is an acronym standing for "Swi3, Ada2, N-Cor, and TFIIIB". It is part of the extended SANT/Myb family. [2]
References
- ^ Horton JR, Elgar SJ, Khan SI, Zhang X, Wade PA, Cheng X (June 2007). "Structure of the SANT domain from the Xenopus chromatin remodeling factor ISWI". Proteins. 67 (4): 1198–202. doi: 10.1002/prot.21352. PMC 2688785. PMID 17377988.
- ^ Boyer LA, Latek RR, Peterson CL (February 2004). "The SANT domain: a unique histone-tail-binding module?". Nature Reviews. Molecular Cell Biology. 5 (2): 158–63. doi: 10.1038/nrm1314. PMID 15040448. S2CID 40665323.
| SANT domain | |
|---|---|
| Identifiers | |
| Symbol | SANT |
| InterPro | IPR017884 |
| PROSITE | PS51293 |
| CATH | 1fex |
| SCOP2 | 1fex / SCOPe / SUPFAM |
In molecular biology, a SANT domain is a protein domain that allows many chromatin remodeling proteins to interact with histones. [1] The name SANT is an acronym standing for "Swi3, Ada2, N-Cor, and TFIIIB". It is part of the extended SANT/Myb family. [2]
References
- ^ Horton JR, Elgar SJ, Khan SI, Zhang X, Wade PA, Cheng X (June 2007). "Structure of the SANT domain from the Xenopus chromatin remodeling factor ISWI". Proteins. 67 (4): 1198–202. doi: 10.1002/prot.21352. PMC 2688785. PMID 17377988.
- ^ Boyer LA, Latek RR, Peterson CL (February 2004). "The SANT domain: a unique histone-tail-binding module?". Nature Reviews. Molecular Cell Biology. 5 (2): 158–63. doi: 10.1038/nrm1314. PMID 15040448. S2CID 40665323.