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2wel

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Revision as of 20:57, 5 August 2016

CRYSTAL STRUCTURE OF SU6656-BOUND CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE II DELTA IN COMPLEX WITH CALMODULIN

Structural highlights

2wel is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	2f3z, 1j7p, 1nkf, 2jl2, 1k93, 1xfv, 1sk6, 1y6w, 1iwq, 1k90, 1yrt, 1lvc, 2w73, 1cll, 1cdl, 1xfy, 1xfu, 2f3y, 1xfx, 1s26, 1j7o, 2w2c, 2vn9, 1yru, 1wrz, 2v02, 1xfz, 1xfw, 2v01, 1pk0, 2be6, 1zot, 2vay, 1sw8, 1aji
Activity:	Calcium/calmodulin-dependent protein kinase, with EC number 2.7.11.17
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Long-term potentiation (LTP), a long-lasting enhancement in communication between neurons, is considered to be the major cellular mechanism underlying learning and memory. LTP triggers high-frequency calcium pulses that result in the activation of Calcium/Calmodulin (CaM)-dependent kinase II (CaMKII). CaMKII acts as a molecular switch because it remains active for a long time after the return to basal calcium levels, which is a unique property required for CaMKII function. Here we describe the crystal structure of the human CaMKIIdelta/Ca2+/CaM complex, structures of all four human CaMKII catalytic domains in their autoinhibited states, as well as structures of human CaMKII oligomerization domains in their tetradecameric and physiological dodecameric states. All four autoinhibited human CaMKIIs were monomeric in the determined crystal structures but associated weakly in solution. In the CaMKIIdelta/Ca2+/CaM complex, the inhibitory region adopted an extended conformation and interacted with an adjacent catalytic domain positioning T287 into the active site of the interacting protomer. Comparisons with autoinhibited CaMKII structures showed that binding of calmodulin leads to the rearrangement of residues in the active site to a conformation suitable for ATP binding and to the closure of the binding groove for the autoinhibitory helix by helix alphaD. The structural data, together with biophysical interaction studies, reveals the mechanism of CaMKII activation by calmodulin and explains many of the unique regulatory properties of these two essential signaling molecules. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3-D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the Web plugin are available in Text S1.

Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation.,Rellos P, Pike AC, Niesen FH, Salah E, Lee WH, von Delft F, Knapp S PLoS Biol. 2010 Jul 27;8(7):e1000426. PMID:20668654^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rellos P, Pike AC, Niesen FH, Salah E, Lee WH, von Delft F, Knapp S. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS Biol. 2010 Jul 27;8(7):e1000426. PMID:20668654 doi:10.1371/journal.pbio.1000426

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wel"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF SU6656-BOUND CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE II DELTA IN COMPLEX WITH CALMODULIN==
 <StructureSection load='2wel' size='340' side='right' caption='[[2wel]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wel]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WEL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wel]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WEL FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K88:(3Z)-N,N-DIMETHYL-2-OXO-3-(4,5,6,7-TETRAHYDRO-1H-INDOL-2-YLMETHYLIDENE)-2,3-DIHYDRO-1H-INDOLE-5-SULFONAMIDE'>K88</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f3z|2f3z]], [[1j7p|1j7p]], [[1nkf|1nkf]], [[2jl2|2jl2]], [[1k93|1k93]], [[1xfv|1xfv]], [[1sk6|1sk6]], [[1y6w|1y6w]], [[1iwq|1iwq]], [[1k90|1k90]], [[1yrt|1yrt]], [[1lvc|1lvc]], [[2w73|2w73]], [[1cll|1cll]], [[1cdl|1cdl]], [[1xfy|1xfy]], [[1xfu|1xfu]], [[2f3y|2f3y]], [[1xfx|1xfx]], [[1s26|1s26]], [[1j7o|1j7o]], [[2w2c|2w2c]], [[2vn9|2vn9]], [[1yru|1yru]], [[1wrz|1wrz]], [[2v02|2v02]], [[1xfz|1xfz]], [[1xfw|1xfw]], [[2v01|2v01]], [[1pk0|1pk0]], [[2be6|2be6]], [[1zot|1zot]], [[2vay|2vay]], [[1sw8|1sw8]], [[1aji|1aji]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium/calmodulin-dependent_protein_kinase Calcium/calmodulin-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.17 2.7.11.17] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wel OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wel RCSB], [http://www.ebi.ac.uk/pdbsum/2wel PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wel OCA], [http://pdbe.org/2wel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wel RCSB], [http://www.ebi.ac.uk/pdbsum/2wel PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wel ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 16: / Line 17: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2wel ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2wel" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 31: / Line 33: @@
 </StructureSection>
 [[Category: Calcium/calmodulin-dependent protein kinase]]
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Arrowsmith, C H]]
 [[Category: Bountra, C]]

2wel

From Proteopedia

Revision as of 20:57, 5 August 2016

CRYSTAL STRUCTURE OF SU6656-BOUND CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE II DELTA IN COMPLEX WITH CALMODULIN

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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