1ctl

From Proteopedia

(Difference between revisions)

Revision as of 10:40, 14 July 2021

STRUCTURE OF THE CARBOXY-TERMINAL LIM DOMAIN FROM THE CYSTEINE RICH PROTEIN CRP

Structural highlights

1ctl is a 1 chain structure with sequence from Chick. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CSRP1_CHICK] Heat stable protein, that interacts with zyxin. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression.

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 solution structure of the carboxy terminal LIM domain of the avian Cysteine Rich Protein (CRP) has been determined by nuclear magnetic resonance spectroscopy. The domain contains two zinc atoms bound independently in CCHC (C = Cys, H = His) and CCCC modules. Both modules contain two orthogonally-arranged antiparallel beta-sheets, and the CCCC module contains an alpha-helix at its C terminus. The modules pack due to hydrophobic interactions forming a novel global fold. The structure of the C-terminal CCCC module is essentially identical to that observed for the DNA-interactive CCCC modules of the GATA-1 and steroid hormone receptor DNA binding domains, raising the possibility that the LIM motif may have a DNA binding function.

Structure of the carboxy-terminal LIM domain from the cysteine rich protein CRP.,Perez-Alvarado GC, Miles C, Michelsen JW, Louis HA, Winge DR, Beckerle MC, Summers MF Nat Struct Biol. 1994 Jun;1(6):388-98. PMID:7664053^[1]

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

References

↑ Perez-Alvarado GC, Miles C, Michelsen JW, Louis HA, Winge DR, Beckerle MC, Summers MF. Structure of the carboxy-terminal LIM domain from the cysteine rich protein CRP. Nat Struct Biol. 1994 Jun;1(6):388-98. PMID:7664053

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/1ctl"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ctl' size='340' side='right'caption='[[1ctl]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ctl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CTL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CTL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ctl]] 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=1CTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CTL FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1ctl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ctl OCA], [http://pdbe.org/1ctl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ctl RCSB], [http://www.ebi.ac.uk/pdbsum/1ctl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ctl 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=1ctl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ctl OCA], [https://pdbe.org/1ctl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ctl RCSB], [https://www.ebi.ac.uk/pdbsum/1ctl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ctl ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CSRP1_CHICK CSRP1_CHICK]] Heat stable protein, that interacts with zyxin. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression.
+[[https://www.uniprot.org/uniprot/CSRP1_CHICK CSRP1_CHICK]] Heat stable protein, that interacts with zyxin. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1ctl

From Proteopedia

Revision as of 10:40, 14 July 2021

STRUCTURE OF THE CARBOXY-TERMINAL LIM DOMAIN FROM THE CYSTEINE RICH PROTEIN CRP

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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