Sandbox Reserved 930: Difference between revisions

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<scene name='57/579700/Adp/5'>ADP</scene> forms hydrogen bonds with the amino acid side chains in the binding pocket, <scene name='57/579700/Mg/5'>Mg2+</scene> coordinates with residues Thr183, Ser 241 of the N-terminal subdomain as well as O1B and O3B from ADP and three water molecules. The hydrogen bonds between ADP and the amino acid residues together with the interactions of Mg2+ keep ADP in the nucleotide-binding pocket.

<scene name='57/579700/Adp/5'>ADP</scene> forms hydrogen bonds with the amino acid side chains in the binding pocket. <scene name='57/579700/Mg/5'>Mg2+</scene> coordinates with residues Thr183, Ser 241 of the N-terminal subdomain as well as O1B and O3B from ADP and three water molecules. The hydrogen bonds between ADP and the amino acid residues together with the interactions of Mg2+ keep ADP in the nucleotide-binding pocket.

In the contractile cycle ATP binding causes a conformational change, which detaches the myosin S1 unit from actin. Then the active site closes, and ATP is hydrolysed to Pi and ADP, leading to the subsequent reattachment of the S1 with the actin. The conformational changes of the acting-binding pocket and the opening and closing of the nucleotide-binding pocket cause the strong and weak acting binding states of myosin, allowing muscle contraction <ref name="houdusse2000"> PMID: 11016966</ref>.

Sandbox Reserved 930: Difference between revisions

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Revision as of 20:14, 18 May 2014 view source Student (talk \| contribs) students 33,923 edits No edit summary ← Older edit		Revision as of 20:23, 18 May 2014 view source Student (talk \| contribs) students 33,923 edits No edit summary Newer edit →
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	<scene name='57/579700/Adp/5'>ADP</scene> forms hydrogen bonds with the amino acid side chains in the binding pocket, <scene name='57/579700/Mg/5'>Mg2+</scene> coordinates with residues Thr183, Ser 241 of the N-terminal subdomain as well as O1B and O3B from ADP and three water molecules. The hydrogen bonds between ADP and the amino acid residues together with the interactions of Mg2+ keep ADP in the nucleotide-binding pocket.		<scene name='57/579700/Adp/5'>ADP</scene> forms hydrogen bonds with the amino acid side chains in the binding pocket. <scene name='57/579700/Mg/5'>Mg2+</scene> coordinates with residues Thr183, Ser 241 of the N-terminal subdomain as well as O1B and O3B from ADP and three water molecules. The hydrogen bonds between ADP and the amino acid residues together with the interactions of Mg2+ keep ADP in the nucleotide-binding pocket.

	In the contractile cycle ATP binding causes a conformational change, which detaches the myosin S1 unit from actin. Then the active site closes, and ATP is hydrolysed to Pi and ADP, leading to the subsequent reattachment of the S1 with the actin. The conformational changes of the acting-binding pocket and the opening and closing of the nucleotide-binding pocket cause the strong and weak acting binding states of myosin, allowing muscle contraction <ref name="houdusse2000"> PMID: 11016966</ref>.		In the contractile cycle ATP binding causes a conformational change, which detaches the myosin S1 unit from actin. Then the active site closes, and ATP is hydrolysed to Pi and ADP, leading to the subsequent reattachment of the S1 with the actin. The conformational changes of the acting-binding pocket and the opening and closing of the nucleotide-binding pocket cause the strong and weak acting binding states of myosin, allowing muscle contraction <ref name="houdusse2000"> PMID: 11016966</ref>.