4cc3: Difference between revisions
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{{STRUCTURE_4cc3| PDB=4cc3 | SCENE= }} | |||
===Complex of human Tuba C-terminal SH3 domain and Mena proline-rich peptide - H3=== | |||
==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> | |||
==About this Structure== | |||
[[4cc3]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CC3 OCA]. | |||
==Reference== | |||
<references group="xtra"/><references/> | |||
[[Category: Homo sapiens]] | |||
[[Category: Ireton, K.]] | |||
[[Category: Julian, R.]] | |||
[[Category: Polle, L.]] | |||
[[Category: Rigano, L.]] | |||
[[Category: Schubert, W D.]] | |||
[[Category: Actin cytoskeleton]] | |||
[[Category: Cortical tension]] | |||
[[Category: Mena]] | |||
[[Category: Ndpp-1]] | |||
[[Category: Proline- rich peptide]] | |||
[[Category: Sh3 domain]] | |||
[[Category: Src homology 3]] | |||
[[Category: Structural protein]] | |||
[[Category: Tuba]] | |||
Revision as of 12:48, 30 October 2013
Complex of human Tuba C-terminal SH3 domain and Mena proline-rich peptide - H3Complex of human Tuba C-terminal SH3 domain and Mena proline-rich peptide - H3
FunctionFunction
[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]
About this StructureAbout this Structure
4cc3 is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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