1cfc

From Proteopedia

(Difference between revisions)

Current revision

CALCIUM-FREE CALMODULIN

Structural highlights

1cfc is a 1 chain structure with sequence from Xenopus laevis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CALM1_XENLA 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.

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

The three-dimensional structure of calmodulin in the absence of Ca2+ has been determined by three- and four-dimensional heteronuclear NMR experiments, including ROE, isotope-filtering combined with reverse labelling, and measurement of more than 700 three-bond J-couplings. In analogy with the Ca(2+)-ligated state of this protein, it consists of two small globular domains separated by a flexible linker, with no stable, direct contacts between the two domains. In the absence of Ca2+, the four helices in each of the two globular domains form a highly twisted bundle, capped by a short anti-parallel beta-sheet. This arrangement is qualitatively similar to that observed in the crystal structure of the Ca(2+)-free N-terminal domain of troponin C.

Solution structure of calcium-free calmodulin.,Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Klee CB, Bax A Nat Struct Biol. 1995 Sep;2(9):768-76. PMID:7552748^[1]

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

References

↑ Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Klee CB, Bax A. Solution structure of calcium-free calmodulin. Nat Struct Biol. 1995 Sep;2(9):768-76. PMID:7552748

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cfc"

@@ Line 1: / Line 1: @@
 ==CALCIUM-FREE CALMODULIN==
-<StructureSection load='1cfc' size='340' side='right'caption='[[1cfc]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
+<StructureSection load='1cfc' size='340' side='right'caption='[[1cfc]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1cfc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CFC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1cfc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CFC FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cfd|1cfd]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1cfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfc OCA], [http://pdbe.org/1cfc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cfc RCSB], [http://www.ebi.ac.uk/pdbsum/1cfc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cfc ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfc OCA], [https://pdbe.org/1cfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cfc RCSB], [https://www.ebi.ac.uk/pdbsum/1cfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cfc ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CALM_XENLA CALM_XENLA]] 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.
+[https://www.uniprot.org/uniprot/CALM1_XENLA CALM1_XENLA] 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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Calmodulin|Calmodulin]]
 *[[Calmodulin 3D structures|Calmodulin 3D structures]]
 *[[Hydrogen in macromolecular models|Hydrogen in macromolecular models]]
-*[[NMR Ensembles of Models|NMR Ensembles of Models]]
-*[[Structural alignment tools|Structural alignment tools]]
 == References ==
 <references/>
@@ Line 41: / Line 38: @@
 [[Category: Large Structures]]
 [[Category: Xenopus laevis]]
-[[Category: Bax, A]]
+[[Category: Bax A]]
-[[Category: Grzesiek, S]]
+[[Category: Grzesiek S]]
-[[Category: Klee, C B]]
+[[Category: Klee CB]]
-[[Category: Kuboniwa, H]]
+[[Category: Kuboniwa H]]
-[[Category: Ren, H]]
+[[Category: Ren H]]
-[[Category: Tjandra, N]]
+[[Category: Tjandra N]]
-[[Category: Calcium-binding protein]]

1cfc

From Proteopedia

Current revision

CALCIUM-FREE CALMODULIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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