Sandbox Reserved 1103: Difference between revisions
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==Your Heading Here (maybe something like 'Structure')== | |||
<Structure load='Insert PDB code or filename here' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | |||
== Function == | == Function == | ||
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== Structure == | == Structure == | ||
<Structure load='Dimer2.pdb' size='350' frame='false' align='centre' scene='82/829356/Dimer/3'>''3BQO TRF1 TRFH domain and TIN2 peptide complex''' | |||
The 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 <scene name='82/829356/Dimer/3'>homodimer</scene>. The two monomers are antiparallel and form a homodimer which is symmetrical. There are three α-helices from each monomer involved in this homodimerization: the helices 1, 2 and 9. 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 Trp77 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 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 <scene name='82/829356/Dimer/3'>homodimer</scene>. The two monomers are antiparallel and form a homodimer which is symmetrical. There are three α-helices from each monomer involved in this homodimerization: the helices 1, 2 and 9. 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 Trp77 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. | ||
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== Structural highlights == | == Structural highlights == | ||
== References == | == References == | ||
