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2f2p

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Revision as of 02:09, 16 November 2017

Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode

Structural highlights

2f2p is a 2 chain structure with sequence from Bovin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2f2o
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CALM_BOVIN] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (By similarity).

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

Calcineurin is a calmodulin-binding protein in brain and the only serine/threonine protein phosphatase under the control of Ca2+/calmodulin (CaM), which plays a critical role in coupling Ca2+ signals to cellular responses. CaM up-regulates the phosphatase activity of calcineurin by binding to the CaM-binding domain (CBD) of calcineurin subunit A. Here, we report crystal structural studies of CaM bound to a CBD peptide. The chimeric protein containing CaM and the CBD peptide forms an intimate homodimer, in which CaM displays a native-like extended conformation and the CBD peptide shows alpha-helical structure. Unexpectedly, the N-terminal lobe from one CaM and the C-terminal lobe from the second molecule form a combined binding site to trap the peptide. Thus, the dimer provides two binding sites, each of which is reminiscent of the fully collapsed conformation of CaM commonly observed in complex with, for example, the myosin light chain kinase (MLCK) peptide. The interaction between the peptide and CaM is highly specific and similar to MLCK.

Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode.,Ye Q, Li X, Wong A, Wei Q, Jia Z Biochemistry. 2006 Jan 24;45(3):738-45. PMID:16411749^[1]

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

References

↑ Ye Q, Li X, Wong A, Wei Q, Jia Z. Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode. Biochemistry. 2006 Jan 24;45(3):738-45. PMID:16411749 doi:10.1021/bi0521801

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2f2p"

@@ Line 1: / Line 1: @@
 ==Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode==
 <StructureSection load='2f2p' size='340' side='right' caption='[[2f2p]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f2o|2f2o]]</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=2f2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f2p OCA], [http://pdbe.org/2f2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f2p RCSB], [http://www.ebi.ac.uk/pdbsum/2f2p 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=2f2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f2p OCA], [http://pdbe.org/2f2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f2p RCSB], [http://www.ebi.ac.uk/pdbsum/2f2p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2f2p ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 2f2p" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Calmodulin|Calmodulin]]
 == References ==
 <references/>
@@ Line 40: / Line 38: @@
 [[Category: Ye, Q]]
 [[Category: Calcineurin]]
+[[Category: Calcium]]
 [[Category: Calmodulin]]
 [[Category: Ef-hand]]
 [[Category: Metal binding protein]]

2f2p

From Proteopedia

Revision as of 02:09, 16 November 2017

Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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