Sandbox Reserved 1103: Difference between revisions

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== Structure ==

The [https://en.wikipedia.org/wiki/TERF1 TRF1] TRFH domain is a sequence motif of about 200 amino acids located in the centre of TRF1. It is entirely constituted of α helices and binds to another TRF1 TRFH to form a homodimer. The two monomers are antiparallel and form a homodimer which is symmetrical. There are three α-helices from each monomer involved in this homodimerization: <scene name='82/829356/Helices_1/1'>the helices 1</scene>, <scene name='82/829356/Helices_2/1'>2</scene> <scene name='82/829356/Helices_9/1'>9</scene>. To form a dimer, the helix 1 of one monomer comes into contact with helix 1 of the other monomer, its helix 2 does it with the helix 2, and so does the helix 9. The two helices 9 stabilize the dimer interface and are perpendicular to the helices 1, forming a cross brace at the top and the bottom of it. The two helices 1 are the core of the dimer interface. This interface involves many hydrophobic interactions and a few hydrogen bonds. The amino acids <scene name='82/829356/Trp77/3'>Trp77</scene> of each helix 1 are central to the formation of the hydrophobic core. “Trp77 packs against Phe255 (helix 9) within the monomer and between Ala259 and Ala260 and against Val263 of helix 9 from its partner” (Fairall L et al Mol Cell.<ref>PMID: 11545737</ref>) The hydrogen bonds involved in the dimer interface are formed between Glu71 of one monomer with Ser85 of the other monomer. Overall, this dimer interface is highly hydrophobic and packed.

The [https://en.wikipedia.org/wiki/TERF1 TRF1] TRFH domain is a sequence motif of about 200 amino acids located in the centre of TRF1. It is entirely constituted of α helices and binds to another TRF1 TRFH to form a homodimer. The two monomers are antiparallel and form a homodimer which is symmetrical. There are three α-helices from each monomer involved in this homodimerization: <scene name='82/829356/Helices_1/1'>the helices 1</scene>, <scene name='82/829356/Helices_2/1'>2</scene> <scene name='82/829356/Helices_9/1'>9</scene>. To form a dimer, the helix 1 of one monomer comes into contact with helix 1 of the other monomer, its helix 2 does it with the helix 2, and so does the helix 9. The two helices 9 stabilize the dimer interface and are perpendicular to the helices 1, forming a cross brace at the top and the bottom of it. The two helices 1 are the core of the dimer interface. This interface involves many hydrophobic interactions and a few hydrogen bonds. The amino acids <scene name='82/829356/Trp77/3'>Trp77</scene> of each helix 1 are central to the formation of the hydrophobic core. “Trp77 packs against <scene name='82/829356/Phe255/1'>Phe255</scene> (helix 9) within the monomer and between <scene name='82/829356/Ala259/1'>Ala259</scene> and <scene name='82/829356/Ala259/1'>Ala260</scene> and against Val263 of helix 9 from its partner” (Fairall L et al Mol Cell.<ref>PMID: 11545737</ref>) The hydrogen bonds involved in the dimer interface are formed between Glu71 of one monomer with Ser85 of the other monomer. Overall, this dimer interface is highly hydrophobic and packed.

Sandbox Reserved 1103: Difference between revisions

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Revision as of 22:21, 14 January 2020 view source Marina Nzepa (talk \| contribs) 64 edits No edit summary ← Older edit		Revision as of 19:10, 15 January 2020 view source Marina Nzepa (talk \| contribs) 64 edits No edit summary Newer edit →
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	== Structure ==		== Structure ==

	The [https://en.wikipedia.org/wiki/TERF1 TRF1] TRFH domain is a sequence motif of about 200 amino acids located in the centre of TRF1. It is entirely constituted of α helices and binds to another TRF1 TRFH to form a homodimer. The two monomers are antiparallel and form a homodimer which is symmetrical. There are three α-helices from each monomer involved in this homodimerization: <scene name='82/829356/Helices_1/1'>the helices 1</scene>, <scene name='82/829356/Helices_2/1'>2</scene> <scene name='82/829356/Helices_9/1'>9</scene>. To form a dimer, the helix 1 of one monomer comes into contact with helix 1 of the other monomer, its helix 2 does it with the helix 2, and so does the helix 9. The two helices 9 stabilize the dimer interface and are perpendicular to the helices 1, forming a cross brace at the top and the bottom of it. The two helices 1 are the core of the dimer interface. This interface involves many hydrophobic interactions and a few hydrogen bonds. The amino acids <scene name='82/829356/Trp77/3'>Trp77</scene> of each helix 1 are central to the formation of the hydrophobic core. “Trp77 packs against Phe255 (helix 9) within the monomer and between Ala259 and Ala260 and against Val263 of helix 9 from its partner” (Fairall L et al Mol Cell.<ref>PMID: 11545737</ref>) The hydrogen bonds involved in the dimer interface are formed between Glu71 of one monomer with Ser85 of the other monomer. Overall, this dimer interface is highly hydrophobic and packed.		The [https://en.wikipedia.org/wiki/TERF1 TRF1] TRFH domain is a sequence motif of about 200 amino acids located in the centre of TRF1. It is entirely constituted of α helices and binds to another TRF1 TRFH to form a homodimer. The two monomers are antiparallel and form a homodimer which is symmetrical. There are three α-helices from each monomer involved in this homodimerization: <scene name='82/829356/Helices_1/1'>the helices 1</scene>, <scene name='82/829356/Helices_2/1'>2</scene> <scene name='82/829356/Helices_9/1'>9</scene>. To form a dimer, the helix 1 of one monomer comes into contact with helix 1 of the other monomer, its helix 2 does it with the helix 2, and so does the helix 9. The two helices 9 stabilize the dimer interface and are perpendicular to the helices 1, forming a cross brace at the top and the bottom of it. The two helices 1 are the core of the dimer interface. This interface involves many hydrophobic interactions and a few hydrogen bonds. The amino acids <scene name='82/829356/Trp77/3'>Trp77</scene> of each helix 1 are central to the formation of the hydrophobic core. “Trp77 packs against <scene name='82/829356/Phe255/1'>Phe255</scene> (helix 9) within the monomer and between <scene name='82/829356/Ala259/1'>Ala259</scene> and <scene name='82/829356/Ala259/1'>Ala260</scene> and against Val263 of helix 9 from its partner” (Fairall L et al Mol Cell.<ref>PMID: 11545737</ref>) The hydrogen bonds involved in the dimer interface are formed between Glu71 of one monomer with Ser85 of the other monomer. Overall, this dimer interface is highly hydrophobic and packed.