2ll2

From Proteopedia

(Difference between revisions)

Revision as of 07:06, 6 May 2020

Structure of the Cx43 C-terminal domain bound to tubulin

Structural highlights

2ll2 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[CXA1_HUMAN] Autosomal recessive non-syndromic sensorineural deafness type DFNB;Hypoplastic left heart syndrome;Oculodentodigital dysplasia;Craniometaphyseal dysplasia;Syndactyly type 3. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease may be caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.

Function

[CXA1_HUMAN] Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by participating in the recycling of potassium to the cochlear endolymph. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract (By similarity).

Publication Abstract from PubMed

Connexins are structurally related transmembrane proteins that assemble to form gap junction channels involved in the mediation of intercellular communication. It has been shown that the intracellular tail of connexin43 (Cx43) interacts with tubulin and microtubules with putative impacts on its own intracellular trafficking, its activity in channel communication, and its interference with specific growth factor signal transduction cascades. We demonstrate here that the microtubule binding of Cx43 is mainly driven by a short region of 26 amino acid residues located within the intracellular tail of Cx43. The nuclear magnetic resonance structural analysis of a peptide (K26D) corresponding to this region shows that this peptide is unstructured when free in solution and adopts a helix conformation upon binding with tubulin. In addition, the resulting K26D-tubulin molecular complex defines a new structural organization that could be shared by other microtubule partners. Interestingly, the K26D-tubulin interaction is prevented by the phosphorylation of K26D at a src kinase specific site. Altogether, the results elucidate the mechanism of the interaction of Cx43 with the microtubule cytoskeleton and propose a pathway for understanding the microtubule-dependent regulation of Cx43 gap junctional communications and the involvement of Cx43 in TGF-beta signal transduction.

Phosphorylation controls the interaction of the connexin43 C-terminal domain with tubulin and microtubules.,Saidi Brikci-Nigassa A, Clement MJ, Ha-Duong T, Adjadj E, Ziani L, Pastre D, Curmi PA, Savarin P Biochemistry. 2012 May 29;51(21):4331-42. Epub 2012 May 14. PMID:22558917^[1]

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

References

↑ Saidi Brikci-Nigassa A, Clement MJ, Ha-Duong T, Adjadj E, Ziani L, Pastre D, Curmi PA, Savarin P. Phosphorylation controls the interaction of the connexin43 C-terminal domain with tubulin and microtubules. Biochemistry. 2012 May 29;51(21):4331-42. Epub 2012 May 14. PMID:22558917 doi:10.1021/bi201806j

1 Structural highlights
2 Disease
3 Function
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/2ll2"

@@ Line 1: / Line 1: @@
 ==Structure of the Cx43 C-terminal domain bound to tubulin==
-<StructureSection load='2ll2' size='340' side='right' caption='[[2ll2]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='2ll2' size='340' side='right'caption='[[2ll2]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ll2]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LL2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ll2]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LL2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2LL2 FirstGlance]. <br>
-</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=2ll2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ll2 OCA], [http://pdbe.org/2ll2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ll2 RCSB], [http://www.ebi.ac.uk/pdbsum/2ll2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ll2 ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2ll2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ll2 OCA], [http://pdbe.org/2ll2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ll2 RCSB], [http://www.ebi.ac.uk/pdbsum/2ll2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ll2 ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 21: / Line 21: @@
 ==See Also==
-*[[Connexin|Connexin]]
+*[[Connexin 3D structure|Connexin 3D structure]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Adjadj, E]]
 [[Category: Benmansour, K]]

2ll2

From Proteopedia

Revision as of 07:06, 6 May 2020

Structure of the Cx43 C-terminal domain bound to tubulin

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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