This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ckk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ckk.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1ckk.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ckk| PDB=1ckk | SCENE= }}
{{STRUCTURE_1ckk| PDB=1ckk | SCENE= }}
-
'''CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT'''
+
===CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT===
-
==Overview==
+
<!--
-
The structure of calcium-bound calmodulin (Ca2+/CaM) complexed with a 26-residue peptide, corresponding to the CaM-binding domain of rat Ca2+/CaM-dependent protein kinase kinase (CaMKK), has been determined by NMR spectroscopy. In this complex, the CaMKK peptide forms a fold comprising an alpha-helix and a hairpin-like loop whose C-terminus folds back on itself. The binding orientation of this CaMKK peptide by the two CaM domains is opposite to that observed in all other CaM-target complexes determined so far. The N- and C-terminal hydrophobic pockets of Ca2+/CaM anchor Trp 444 and Phe 459 of the CaMKK peptide, respectively. This 14-residue separation between two key hydrophobic groups is also unique among previously determined CaM complexes. The present structure represents a new and distinct class of Ca2+/CaM target recognition that may be shared by other Ca2+/CaM-stimulated proteins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10467092}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10467092 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10467092}}
==About this Structure==
==About this Structure==
-
1CKK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKK OCA].
+
1CKK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKK OCA].
==Reference==
==Reference==
Line 34: Line 38:
[[Category: Camkk]]
[[Category: Camkk]]
[[Category: Nmr]]
[[Category: Nmr]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:49:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:52:30 2008''

Revision as of 17:52, 30 June 2008

Template:STRUCTURE 1ckk

CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT

Template:ABSTRACT PUBMED 10467092

About this Structure

1CKK is a Single protein structure of sequence from Rattus norvegicus and Xenopus laevis. Full experimental information is available from OCA.

Reference

A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase., Osawa M, Tokumitsu H, Swindells MB, Kurihara H, Orita M, Shibanuma T, Furuya T, Ikura M, Nat Struct Biol. 1999 Sep;6(9):819-24. PMID:10467092

Page seeded by OCA on Mon Jun 30 20:52:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ckk"
Personal tools