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.


1dtl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1dtl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dtl, resolution 2.15&Aring;" /> '''CRYSTAL STRUCTURE OF...)
Current revision (05:57, 9 August 2023) (edit) (undo)
 
(18 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1dtl.gif|left|200px]]<br /><applet load="1dtl" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1dtl, resolution 2.15&Aring;" />
 
-
'''CRYSTAL STRUCTURE OF CALCIUM-SATURATED (3CA2+) CARDIAC TROPONIN C COMPLEXED WITH THE CALCIUM SENSITIZER BEPRIDIL AT 2.15 A RESOLUTION'''<br />
 
-
==Overview==
+
==CRYSTAL STRUCTURE OF CALCIUM-SATURATED (3CA2+) CARDIAC TROPONIN C COMPLEXED WITH THE CALCIUM SENSITIZER BEPRIDIL AT 2.15 A RESOLUTION==
-
Cardiac troponin C (cTnC) is the calcium-dependent switch for contraction, in heart muscle and a potential target for drugs in the therapy of, congestive heart failure. This calmodulin-like protein consists of two, lobes connected by a central linker; each lobe contains two EF-hand, domains. The regulatory N-terminal lobe of cTnC, unlike that of skeletal, troponin C (sTnC), contains only one functional EF-hand and does not open, fully upon the binding of Ca(2+). We have determined the crystal structure, of cTnC, with three bound Ca(2+) ions, complexed with the, calcium-sensitizer bepridil, to 2.15-A resolution. In contrast to apo- and, 3Ca(2+)-cTnC, the drug-bound complex displays a fully open N-terminal lobe, similar to the N-terminal lobes of 4Ca(2+)-sTnC and cTnC bound to a, C-terminal fragment of cardiac troponin I (residues 147-163). The closing, of the lobe is sterically hindered by one of the three bound bepridils., Our results provide a structural basis for the Ca(2+)-sensitizing effect, of bepridil and reveal the details of a distinctive two-stage mechanism, for Ca(2+) regulation by troponin C in cardiac muscle.
+
<StructureSection load='1dtl' size='340' side='right'caption='[[1dtl]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1dtl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DTL FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEP:1-ISOBUTOXY-2-PYRROLIDINO-3[N-BENZYLANILINO]+PROPANE'>BEP</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=1dtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dtl OCA], [https://pdbe.org/1dtl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dtl RCSB], [https://www.ebi.ac.uk/pdbsum/1dtl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dtl ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/TNNC1_CHICK TNNC1_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]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dt/1dtl_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<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/main_output.php?pdb_ID=1dtl ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Cardiac troponin C (cTnC) is the calcium-dependent switch for contraction in heart muscle and a potential target for drugs in the therapy of congestive heart failure. This calmodulin-like protein consists of two lobes connected by a central linker; each lobe contains two EF-hand domains. The regulatory N-terminal lobe of cTnC, unlike that of skeletal troponin C (sTnC), contains only one functional EF-hand and does not open fully upon the binding of Ca(2+). We have determined the crystal structure of cTnC, with three bound Ca(2+) ions, complexed with the calcium-sensitizer bepridil, to 2.15-A resolution. In contrast to apo- and 3Ca(2+)-cTnC, the drug-bound complex displays a fully open N-terminal lobe similar to the N-terminal lobes of 4Ca(2+)-sTnC and cTnC bound to a C-terminal fragment of cardiac troponin I (residues 147-163). The closing of the lobe is sterically hindered by one of the three bound bepridils. Our results provide a structural basis for the Ca(2+)-sensitizing effect of bepridil and reveal the details of a distinctive two-stage mechanism for Ca(2+) regulation by troponin C in cardiac muscle.
-
==About this Structure==
+
Bepridil opens the regulatory N-terminal lobe of cardiac troponin C.,Li Y, Love ML, Putkey JA, Cohen C Proc Natl Acad Sci U S A. 2000 May 9;97(10):5140-5. PMID:10792039<ref>PMID:10792039</ref>
-
1DTL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CA and BEP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DTL OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Bepridil opens the regulatory N-terminal lobe of cardiac troponin C., Li Y, Love ML, Putkey JA, Cohen C, Proc Natl Acad Sci U S A. 2000 May 9;97(10):5140-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10792039 10792039]
+
</div>
-
[[Category: Gallus gallus]]
+
<div class="pdbe-citations 1dtl" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Cohen, C.]]
+
-
[[Category: Li, Y.]]
+
-
[[Category: Love, M.L.]]
+
-
[[Category: Putkey, J.A.]]
+
-
[[Category: BEP]]
+
-
[[Category: CA]]
+
-
[[Category: helix-turn-helix]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:34:11 2007''
+
==See Also==
 +
*[[Troponin 3D structures|Troponin 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Gallus gallus]]
 +
[[Category: Large Structures]]
 +
[[Category: Cohen C]]
 +
[[Category: Li Y]]
 +
[[Category: Love ML]]
 +
[[Category: Putkey JA]]

Current revision

CRYSTAL STRUCTURE OF CALCIUM-SATURATED (3CA2+) CARDIAC TROPONIN C COMPLEXED WITH THE CALCIUM SENSITIZER BEPRIDIL AT 2.15 A RESOLUTION

PDB ID 1dtl

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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