Sandbox Reserved 815: Difference between revisions

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The protein exists in majority in its dimer form.  
The protein exists in majority in its dimer form.  
Between each <scene name='User:Erin_May/Sandbox_1/Nonpolar_at_dimer_interface/2'>helix 144-156</scene> of the two proteins, it exists many interactions whose stabilize the dimer interface. It can be retain acidic and mostly negative residues, or basic and positive residues.
Between each <scene name='User:Erin_May/Sandbox_1/Nonpolar_at_dimer_interface/2'>helix 144-156</scene> of the two proteins, it exists many interactions whose stabilize the dimer interface. It can be retain acidic and mostly negative residues, or basic and positive residues.
Each <scene name='User:Erin_May/Sandbox_1/Helix_2_with_helix_3/1'>helix 171−188</scene> is linked to the C-terminal helix 200−225 of the other monomer. [http://en.wikipedia.org/wiki/Van_der_Waals_forces Van der Waals] forces are here between such nonpolar residues as valine, isoleucine, and nonpolar sections as histadine, methionine, and glutamic acid.
Each is linked to the C-terminal helix 200−225 of the other monomer. [http://en.wikipedia.org/wiki/Van_der_Waals_forces Van der Waals] forces are here between such nonpolar residues as valine, isoleucine, and nonpolar sections as histadine, methionine, and glutamic acid.
It occurs <scene name='User:Erin_May/Sandbox_1/Interface_hydrogen_bonding/1'> hydrogen bonding</scene> between the dimers at Thr188 O−Gly195 N, Thr190 O−Lys194 N and Thr192 O−Thr192 N
It occurs hydrogen bonding between the dimers at Thr188 O−Gly195 N, Thr190 O−Lys194 N and Thr192 O−Thr192 N
On each monomer, a <scene name='User:Erin_May/Sandbox_1/Hydrogen_bond_asp_202/1'>Hydrogen bond</scene> between Asp 202 and Thr 199 stabilize the dimeric structure.
On each monomer, a Hydrogen bond between Asp 202 and Thr 199 stabilize the dimeric structure.
Arg 220 and Ser 132 form a <scene name='User:Erin_May/Sandbox_1/Hydrogen bond/1'> located at the end of helix 3 which permit the inter-chain interactions to be specific.
Arg 220 and Ser 132 form a Hydrogen bond located at the end of helix 3 which permit the inter-chain interactions to be specific.


The entire 3haf domain can interact with [http://en.wikipedia.org/wiki/GRB2 Growth factor receptor-bound protein 2] (GRB2), [http://en.wikipedia.org/wiki/Exoribonuclease exoribonuclease 3](ERI3) and [http://en.wikipedia.org/wiki/Synapsin_I Synapsin I] (SYN1).
The entire 3haf domain can interact with [http://en.wikipedia.org/wiki/GRB2 Growth factor receptor-bound protein 2] (GRB2), [http://en.wikipedia.org/wiki/Exoribonuclease exoribonuclease 3](ERI3) and [http://en.wikipedia.org/wiki/Synapsin_I Synapsin I] (SYN1).
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