4cc3

From Proteopedia

(Difference between revisions)

Revision as of 19:57, 25 December 2014

Complex of human Tuba C-terminal SH3 domain and Mena proline-rich peptide - H3

Structural highlights

4cc3 is a 8 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4cc2, 4cc4
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[DNMBP_HUMAN] Scaffold protein that links dynamin with actin-regulating proteins. May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). [ENAH_MOUSE] Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

The human pathogen Listeria monocytogenes is able to directly spread to neighboring cells of host tissues, a process recently linked to the virulence factor InlC. InlC targets the sixth SH3 domain (SH3-6) of human Tuba, disrupting its physiological interaction with the cytoskeletal protein N-WASP. The resulting loss of cortical actin tension may slacken the junctional membrane, allowing protrusion formation by motile Listeria. Complexes of Tuba SH3-6 with physiological partners N-WASP and Mena reveal equivalent binding modes but distinct affinities. The interaction surface of the infection complex InlC/Tuba SH3-6 is centered on phenylalanine 146 of InlC stacking upon asparagine 1569 of Tuba. Replacing Phe146 by alanine largely abrogates molecular affinity and in vivo mimics deletion of inlC. Collectively, our findings indicate that InlC hijacks Tuba through its LRR domain, blocking the peptide binding groove to prevent recruitment of its physiological partners.

Structural Details of Human Tuba Recruitment by InlC of Listeria monocytogenes Elucidate Bacterial Cell-Cell Spreading.,Polle L, Rigano LA, Julian R, Ireton K, Schubert WD Structure. 2013 Dec 10. pii: S0969-2126(13)00429-2. doi:, 10.1016/j.str.2013.10.017. PMID:24332715^[5]

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

References

↑ Gertler FB, Niebuhr K, Reinhard M, Wehland J, Soriano P. Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics. Cell. 1996 Oct 18;87(2):227-39. PMID:8861907
↑ Lanier LM, Gates MA, Witke W, Menzies AS, Wehman AM, Macklis JD, Kwiatkowski D, Soriano P, Gertler FB. Mena is required for neurulation and commissure formation. Neuron. 1999 Feb;22(2):313-25. PMID:10069337
↑ Loureiro JJ, Rubinson DA, Bear JE, Baltus GA, Kwiatkowski AV, Gertler FB. Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena/vasodilator-stimulated phosphoprotein (VASP) function during cell migration. Mol Biol Cell. 2002 Jul;13(7):2533-46. PMID:12134088 doi:http://dx.doi.org/10.1091/mbc.E01-10-0102
↑ Lebrand C, Dent EW, Strasser GA, Lanier LM, Krause M, Svitkina TM, Borisy GG, Gertler FB. Critical role of Ena/VASP proteins for filopodia formation in neurons and in function downstream of netrin-1. Neuron. 2004 Apr 8;42(1):37-49. PMID:15066263
↑ Polle L, Rigano LA, Julian R, Ireton K, Schubert WD. Structural Details of Human Tuba Recruitment by InlC of Listeria monocytogenes Elucidate Bacterial Cell-Cell Spreading. Structure. 2013 Dec 10. pii: S0969-2126(13)00429-2. doi:, 10.1016/j.str.2013.10.017. PMID:24332715 doi:http://dx.doi.org/10.1016/j.str.2013.10.017

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4cc3"

@@ Line 7: / Line 7: @@
 <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=4cc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cc3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cc3 RCSB], [http://www.ebi.ac.uk/pdbsum/4cc3 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/DNMBP_HUMAN DNMBP_HUMAN]] Scaffold protein that links dynamin with actin-regulating proteins. May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). [[http://www.uniprot.org/uniprot/ENAH_MOUSE ENAH_MOUSE]] Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation.<ref>PMID:8861907</ref> <ref>PMID:10069337</ref> <ref>PMID:12134088</ref> <ref>PMID:15066263</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4cc3

From Proteopedia

Revision as of 19:57, 25 December 2014

Complex of human Tuba C-terminal SH3 domain and Mena proline-rich peptide - H3

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox