1h67

From Proteopedia

(Difference between revisions)

Current revision

NMR Structure of the CH Domain of Calponin

Structural highlights

1h67 is a 1 chain structure with sequence from Gallus gallus. 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

CNN1_CHICK Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.

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

Calponin is involved in the regulation of contractility and organization of the actin cytoskeleton in smooth muscle cells. It is the archetypal member of the calponin homology (CH) domain family of actin binding proteins that includes cytoskeletal linkers such as alpha-actinin, spectrin, and dystrophin, and regulatory proteins including VAV, IQGAP, and calponin. We have determined the first structure of a CH domain from a single CH domain-containing protein, that of calponin, and have fitted the NMR-derived coordinates to the 3D-helical reconstruction of the F-actin:calponin complex using cryo-electron microscopy. The tertiary fold of this single CH domain is typical of, yet significantly different from, those of the CH domains that occur in tandem pairs to form high-affinity ABDs in other proteins. We thus provide a structural insight into the mode of interaction between F-actin and CH domain-containing proteins.

Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin:calponin.,Bramham J, Hodgkinson JL, Smith BO, Uhrin D, Barlow PN, Winder SJ Structure. 2002 Feb;10(2):249-58. PMID:11839310^[1]

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

References

↑ Bramham J, Hodgkinson JL, Smith BO, Uhrin D, Barlow PN, Winder SJ. Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin:calponin. Structure. 2002 Feb;10(2):249-58. PMID:11839310

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/1h67"

@@ Line 1: / Line 1: @@
 ==NMR Structure of the CH Domain of Calponin==
-<StructureSection load='1h67' size='340' side='right'caption='[[1h67]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1h67' size='340' side='right'caption='[[1h67]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1h67]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H67 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1h67]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H67 FirstGlance]. <br>
-</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=1h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h67 OCA], [https://pdbe.org/1h67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h67 RCSB], [https://www.ebi.ac.uk/pdbsum/1h67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h67 ProSAT]</span></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'>[https://proteopedia.org/fgij/fg.htm?mol=1h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h67 OCA], [https://pdbe.org/1h67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h67 RCSB], [https://www.ebi.ac.uk/pdbsum/1h67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h67 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CNN1_CHICK CNN1_CHICK]] Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.
+[https://www.uniprot.org/uniprot/CNN1_CHICK CNN1_CHICK] Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Chick]]
+[[Category: Gallus gallus]]
 [[Category: Large Structures]]
-[[Category: Barlow, P N]]
+[[Category: Barlow PN]]
-[[Category: Bramham, J]]
+[[Category: Bramham J]]
-[[Category: Smith, B O]]
+[[Category: Smith BO]]
-[[Category: Uhrin, D]]
+[[Category: Uhrin D]]
-[[Category: Winder, S J]]
+[[Category: Winder SJ]]
-[[Category: Actin binding]]
-[[Category: Calponin homology domain]]
-[[Category: Cytoskeleton]]

1h67

From Proteopedia

Current revision

NMR Structure of the CH Domain of Calponin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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