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1oeb
From Proteopedia
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MONA/GADS SH3C DOMAIN
Overview
SH3 domains are protein recognition modules within many adaptors and, enzymes. With more than 500 SH3 domains in the human genome, binding, selectivity is a key issue in understanding the molecular basis of SH3, domain interactions. The Grb2-like adaptor protein Mona/Gads associates, stably with the T-cell receptor signal transducer SLP-76. The crystal, structure of a complex between the C-terminal SH3 domain (SH3C) of, Mona/Gads and a SLP-76 peptide has now been solved to 1.7 A. The peptide, lacks the canonical SH3 domain binding motif P-x-x-P and does not form a, frequently observed poly-proline type II helix. Instead, it adopts a, clamp-like shape around the circumfence of the SH3C beta-barrel. The, central R-x-x-K motif of the peptide forms a 3(10) helix and inserts into, a negatively ... [(full description)]
About this Structure
1OEB is a [Protein complex] structure of sequences from [Mus musculus] with CD as [ligand]. Structure known Active Site: CD1. Full crystallographic information is available from [OCA].
Reference
Structural basis for SH3 domain-mediated high-affinity binding between Mona/Gads and SLP-76., Harkiolaki M, Lewitzky M, Gilbert RJ, Jones EY, Bourette RP, Mouchiroud G, Sondermann H, Moarefi I, Feller SM, EMBO J. 2003 Jun 2;22(11):2571-82. PMID:12773374
Page seeded by OCA on Tue Oct 30 15:51:28 2007
Categories: Mus musculus | Protein complex | Bourette, R.P. | Feller, S.M. | Gilbert, R.J.C. | Harkiolaki, M. | Jones, E.Y. | Lewitzky, M. | Moarefi, I. | Mouchiroud, G. | Sondermann, H. | CD | Dimer | Gads | Mona | Sh3 | Signal tranduction | Slp-76
