We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1rgs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1rgs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rgs, resolution 2.8&Aring;" /> '''REGULATORY SUBUNIT OF...)
Line 1: Line 1:
-
[[Image:1rgs.gif|left|200px]]<br /><applet load="1rgs" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1rgs.gif|left|200px]]<br /><applet load="1rgs" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1rgs, resolution 2.8&Aring;" />
caption="1rgs, resolution 2.8&Aring;" />
'''REGULATORY SUBUNIT OF CAMP DEPENDENT PROTEIN KINASE'''<br />
'''REGULATORY SUBUNIT OF CAMP DEPENDENT PROTEIN KINASE'''<br />
==Overview==
==Overview==
-
In the molecular scheme of living organisms, adenosine 3',5'-monophosphate, (cyclic AMP or cAMP) has been a universal second messenger. In eukaryotic, cells, the primary receptors for cAMP are the regulatory subunits of, cAMP-dependent protein kinase. The crystal structure of a 1-91 deletion, mutant of the type I alpha regulatory subunit was refined to 2.8 A, resolution. Each of the two tandem cAMP binding domains provides an, extensive network of hydrogen bonds that buries the cyclic phosphate and, the ribose between two beta strands that are linked by a short alpha, helix. Each adenine base stacks against an aromatic ring that lies outside, the beta barrel. This structure provides a molecular basis for, understanding how cAMP binds cooperatively to its receptor protein, thus, mediating activation of the kinase.
+
In the molecular scheme of living organisms, adenosine 3',5'-monophosphate (cyclic AMP or cAMP) has been a universal second messenger. In eukaryotic cells, the primary receptors for cAMP are the regulatory subunits of cAMP-dependent protein kinase. The crystal structure of a 1-91 deletion mutant of the type I alpha regulatory subunit was refined to 2.8 A resolution. Each of the two tandem cAMP binding domains provides an extensive network of hydrogen bonds that buries the cyclic phosphate and the ribose between two beta strands that are linked by a short alpha helix. Each adenine base stacks against an aromatic ring that lies outside the beta barrel. This structure provides a molecular basis for understanding how cAMP binds cooperatively to its receptor protein, thus mediating activation of the kinase.
==About this Structure==
==About this Structure==
-
1RGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CMP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RGS OCA].
+
1RGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CMP:'>CMP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RGS OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Dostmann, W.R.G.]]
+
[[Category: Dostmann, W R.G.]]
[[Category: Durick, K.]]
[[Category: Durick, K.]]
-
[[Category: Eyck, L.Ten.]]
+
[[Category: Eyck, L Ten.]]
-
[[Category: Herberg, F.W.]]
+
[[Category: Herberg, F W.]]
[[Category: Su, Y.]]
[[Category: Su, Y.]]
-
[[Category: Taylor, S.S.]]
+
[[Category: Taylor, S S.]]
-
[[Category: Varughese, K.I.]]
+
[[Category: Varughese, K I.]]
-
[[Category: Xuong, N.H.]]
+
[[Category: Xuong, N H.]]
[[Category: CMP]]
[[Category: CMP]]
[[Category: kinase]]
[[Category: kinase]]
[[Category: regulatory subunit]]
[[Category: regulatory subunit]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:35:12 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:46 2008''

Revision as of 12:50, 21 February 2008


1rgs, resolution 2.8Å

Drag the structure with the mouse to rotate

REGULATORY SUBUNIT OF CAMP DEPENDENT PROTEIN KINASE

Overview

In the molecular scheme of living organisms, adenosine 3',5'-monophosphate (cyclic AMP or cAMP) has been a universal second messenger. In eukaryotic cells, the primary receptors for cAMP are the regulatory subunits of cAMP-dependent protein kinase. The crystal structure of a 1-91 deletion mutant of the type I alpha regulatory subunit was refined to 2.8 A resolution. Each of the two tandem cAMP binding domains provides an extensive network of hydrogen bonds that buries the cyclic phosphate and the ribose between two beta strands that are linked by a short alpha helix. Each adenine base stacks against an aromatic ring that lies outside the beta barrel. This structure provides a molecular basis for understanding how cAMP binds cooperatively to its receptor protein, thus mediating activation of the kinase.

About this Structure

1RGS is a Single protein structure of sequence from Bos taurus with as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

Reference

Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains., Su Y, Dostmann WR, Herberg FW, Durick K, Xuong NH, Ten Eyck L, Taylor SS, Varughese KI, Science. 1995 Aug 11;269(5225):807-13. PMID:7638597

Page seeded by OCA on Thu Feb 21 14:50:46 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools