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Testosterone Replacement, Low T, HCG, & Beyond
Testosterone and Men's Health Articles
The Dynamics of Allosteric Binding of Estradiol to SHBG
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<blockquote data-quote="madman" data-source="post: 199559" data-attributes="member: 13851"><p><strong>Figure 5. Dynamic cross-correlation matrices for SHBG dimer illustrate that distant residues in the two monomers are conformationally coupled and respond to the binding of estradiol to either of the two monomers. Inter-monomeric residue motion correlations were examined for the three states: unliganded (5A; SHBG:0E2), Singly bound (5B; SHBG:1E2) and doubly bound (5C; SHBG:2E2). The quadrants depicting the inter-monomer correlation show changes in coordinated movement of the residues in the two monomers. Red color intensity stands for strength of residue correlation. The correlated motions whose absolute values were smaller than 0.3 were not included. The right panels show the location of distant residues at the intermonomeric interface and ligand binding pockets in the two monomers which are conformationally coupled in the respective liganded states. Only the residues, which show correlated movement, are colored in monomer 1 (red) and monomer 2 (blue). Estradiol molecule is represented in purple color. Collectively, these data show that allosteric coupling in binding estradiol is manifested through coordinate, dynamic rearrangement of residues in each of the two SHBG monomers.</strong></p><p><strong>[ATTACH=full]13803[/ATTACH]</strong></p></blockquote><p></p>
[QUOTE="madman, post: 199559, member: 13851"] [B]Figure 5. Dynamic cross-correlation matrices for SHBG dimer illustrate that distant residues in the two monomers are conformationally coupled and respond to the binding of estradiol to either of the two monomers. Inter-monomeric residue motion correlations were examined for the three states: unliganded (5A; SHBG:0E2), Singly bound (5B; SHBG:1E2) and doubly bound (5C; SHBG:2E2). The quadrants depicting the inter-monomer correlation show changes in coordinated movement of the residues in the two monomers. Red color intensity stands for strength of residue correlation. The correlated motions whose absolute values were smaller than 0.3 were not included. The right panels show the location of distant residues at the intermonomeric interface and ligand binding pockets in the two monomers which are conformationally coupled in the respective liganded states. Only the residues, which show correlated movement, are colored in monomer 1 (red) and monomer 2 (blue). Estradiol molecule is represented in purple color. Collectively, these data show that allosteric coupling in binding estradiol is manifested through coordinate, dynamic rearrangement of residues in each of the two SHBG monomers. [ATTACH type="full"]13803[/ATTACH][/B] [/QUOTE]
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Testosterone Replacement, Low T, HCG, & Beyond
Testosterone and Men's Health Articles
The Dynamics of Allosteric Binding of Estradiol to SHBG
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