1s70

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[[Image:1s70.gif|left|200px]]<br /><applet load="1s70" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1s70.gif|left|200px]]
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caption="1s70, resolution 2.70&Aring;" />
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'''Complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (MYPT1)'''<br />
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{{Structure
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|PDB= 1s70 |SIZE=350|CAPTION= <scene name='initialview01'>1s70</scene>, resolution 2.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=PGE:TRIETHYLENE GLYCOL'>PGE</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16]
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|GENE= PPP1CB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (MYPT1)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1S70 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=PGE:'>PGE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S70 OCA].
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1S70 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S70 OCA].
==Reference==
==Reference==
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Structural basis of protein phosphatase 1 regulation., Terrak M, Kerff F, Langsetmo K, Tao T, Dominguez R, Nature. 2004 Jun 17;429(6993):780-4. Epub 2004 May 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15164081 15164081]
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Structural basis of protein phosphatase 1 regulation., Terrak M, Kerff F, Langsetmo K, Tao T, Dominguez R, Nature. 2004 Jun 17;429(6993):780-4. Epub 2004 May 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15164081 15164081]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: pp1]]
[[Category: pp1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:01:18 2008''

Revision as of 12:01, 20 March 2008


PDB ID 1s70

Drag the structure with the mouse to rotate
, resolution 2.70Å
Ligands: and
Gene: PPP1CB (Homo sapiens)
Activity: Phosphoprotein phosphatase, with EC number 3.1.3.16
Coordinates: save as pdb, mmCIF, xml



Complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (MYPT1)


Overview

The coordinated and reciprocal action of serine/threonine (Ser/Thr) protein kinases and phosphatases produces transient phosphorylation, a fundamental regulatory mechanism for many biological processes. The human genome encodes a far greater number of Ser/Thr protein kinases than of phosphatases. Protein phosphatase 1 (PP1), in particular, is ubiquitously distributed and regulates a broad range of cellular functions, including glycogen metabolism, cell-cycle progression and muscle relaxation. PP1 has evolved effective catalytic machinery but lacks substrate specificity. Substrate specificity is conferred upon PP1 through interactions with a large number of regulatory subunits. The regulatory subunits are generally unrelated, but most possess the RVxF motif, a canonical PP1-binding sequence. Here we reveal the crystal structure at 2.7 A resolution of the complex between PP1 and a 34-kDa N-terminal domain of the myosin phosphatase targeting subunit MYPT1. MYPT1 is the protein that regulates PP1 function in smooth muscle relaxation. Structural elements amino- and carboxy-terminal to the RVxF motif of MYPT1 are positioned in a way that leads to a pronounced reshaping of the catalytic cleft of PP1, contributing to the increased myosin specificity of this complex. The structure has general implications for the control of PP1 activity by other regulatory subunits.

About this Structure

1S70 is a Protein complex structure of sequences from Gallus gallus and Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of protein phosphatase 1 regulation., Terrak M, Kerff F, Langsetmo K, Tao T, Dominguez R, Nature. 2004 Jun 17;429(6993):780-4. Epub 2004 May 26. PMID:15164081

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