CD2-associated protein (CD2AP) called also CMS, is a scaffolding protein which regulates actin cytoskeleton. CD2AP SH3 domain interacts with actin and a variety of membrane proteins. CD2AP contains in its N-terminal 3 SH3 domains followed by a proline-rich region.[1][2]
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3D structures of CD2-associated protein3D structures of CD2-associated protein
Updated on 23-November-2015
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- CD2AP SH3 domain 1
- 2j6k – hCD2AP – human
- 2krm – mCD2AP – mouse - NMR
- 2j6f – hCD2AP + E3 ubiquitin protein ligase peptide
- 2j6o, 2j7i – hCD2AP + CD2 peptide
- 2mcn - mCD2AP + ubiquitin
- CD2AP SH3 domain 2
- 2fei – hCD2AP – NMR
- 2krn – mCD2AP – NMR
- 3u23 - hCD2AP + RIN3 proline-rich peptide
- CD2AP SH3 domain 3
- CD2AP proline-rich domain
ReferencesReferences
- ↑ Dikic I. CIN85/CMS family of adaptor molecules. FEBS Lett. 2002 Oct 2;529(1):110-5. PMID:12354621
- ↑ Moncalian G, Cardenes N, Deribe YL, Spinola-Amilibia M, Dikic I, Bravo J. Atypical polyproline recognition by the CMS N-terminal Src homology 3 domain. J Biol Chem. 2006 Dec 15;281(50):38845-53. Epub 2006 Oct 3. PMID:17020880 doi:10.1074/jbc.M606411200
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