1pms

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PLECKSTRIN HOMOLOGY DOMAIN OF SON OF SEVENLESS 1 (SOS1) WITH GLYCINE-SERINE ADDED TO THE N-TERMINUS, NMR, 20 STRUCTURES

Overview

The solution structure of the pleckstrin homology (PH) domain of mouse, Son-of-sevenless 1 (mSos1), a guanine nucleotide exchange factor for Ras, was determined by multidimensional NMR spectroscopy. The structure of the, mSos1 PH domain involves the fundamental PH fold, consisting of seven, beta-strands and one alpha-helix at the C terminus, as determined for the, PH domains of other proteins. By contrast, the mSos1 PH domain showed two, major characteristic features. First, the N-terminal region, whose amino, acid sequence is highly conserved among Sos proteins, was found to form an, alpha-helix, which interacts with the beta-sheet structure of the, fundamental PH fold. Second, there is a long unstructured loop between, beta3 and beta4. Furthermore, the mSos1 PH domain was found to bind, phosphatidylinositol-4,5-bisphosphate by a centrifugation assay. The, addition of inositol-1,4,5-trisphosphate to the mSos1 PH domain induced, backbone amide chemical shift changes mainly in the beta1/beta2 loop and, the N- and C-terminal parts of the long beta3/beta4 loop. This, inositol-1,4,5-trisphosphate-binding mode of the mSos1 PH domain is, somewhat similar to those of the PH domains of pleckstrin and, phospholipase Cdelta1, and is clearly different from those of other PH, domains.

About this Structure

1PMS is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The solution structure of the pleckstrin homology domain of mouse Son-of-sevenless 1 (mSos1)., Koshiba S, Kigawa T, Kim JH, Shirouzu M, Bowtell D, Yokoyama S, J Mol Biol. 1997 Jun 20;269(4):579-91. PMID:9217262

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