1avs

From Proteopedia

(Difference between revisions)

Revision as of 06:54, 24 February 2021

X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C

Structural highlights

1avs is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TNNC2_CHICK] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.

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

We have solved and refined the crystal and molecular structures of the calcium-saturated N-terminal domain of troponin C (TnC) to 1.75 A resolution. This has allowed for the first detailed analysis of the calcium binding sites of this molecular switch in the calcium-loaded state. The results provide support for the proposed binding order and qualitatively, for the affinity of calcium in the two regulatory calcium binding sites. Based on a comparison with the high-resolution apo-form of TnC we propose a possible mechanism for the calcium-mediated exposure of a large hydrophobic surface that is central to the initiation of muscle contraction within the cell.

Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 A resolution.,Strynadka NC, Cherney M, Sielecki AR, Li MX, Smillie LB, James MN J Mol Biol. 1997 Oct 17;273(1):238-55. PMID:9367759^[1]

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

References

↑ Strynadka NC, Cherney M, Sielecki AR, Li MX, Smillie LB, James MN. Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 A resolution. J Mol Biol. 1997 Oct 17;273(1):238-55. PMID:9367759 doi:http://dx.doi.org/10.1006/jmbi.1997.1257

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/1avs"

@@ Line 3: / Line 3: @@
 <StructureSection load='1avs' size='340' side='right'caption='[[1avs]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1avs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AVS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1avs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AVS 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></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1avs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1avs OCA], [http://pdbe.org/1avs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1avs RCSB], [http://www.ebi.ac.uk/pdbsum/1avs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1avs 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=1avs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1avs OCA], [https://pdbe.org/1avs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1avs RCSB], [https://www.ebi.ac.uk/pdbsum/1avs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1avs ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TNNC2_CHICK TNNC2_CHICK]] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
+[[https://www.uniprot.org/uniprot/TNNC2_CHICK TNNC2_CHICK]] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1avs

From Proteopedia

Revision as of 06:54, 24 February 2021

X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C

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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