From: Subject: Molecular Cell -- Babon et al. Date: Fri, 28 Apr 2006 12:32:34 +0200 MIME-Version: 1.0 Content-Type: multipart/related; type="text/html"; boundary="----=_NextPart_000_0000_01C66ABF.D3303ED0" X-MimeOLE: Produced By Microsoft MimeOLE V6.00.2900.2869 This is a multi-part message in MIME format. ------=_NextPart_000_0000_01C66ABF.D3303ED0 Content-Type: text/html; charset="utf-8" Content-Transfer-Encoding: quoted-printable Content-Location: http://www.molecule.org/content/article/abstract?uid=PIIS1097276506001900&highlight=babon =EF=BB=BF Molecular Cell -- Babon et = al.

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Article

The Structure of SOCS3 = Reveals the=20 Basis of the Extended SH2 Domain Function and Identifies an = Unstructured=20 Insertion That Regulates Stability

Jeffrey=20 J. Babon,^¹,Edward=20 J. McManus,^¹=20Shenggen Yao,^¹=20David=20 P. DeSouza,^¹,³=20Lisa=20 A. Mielke,^¹=20Naomi=20 S. Sprigg,^¹=20Tracy=20 A. Willson,^¹=20Douglas=20 J. Hilton,^¹=20Nicos=20 A. Nicola,^¹=20Manuel Baca,^²=20Sandra=20 E. Nicholson,^¹=20and Raymond=20 S. Norton^¹=20

1 The = Walter and=20 Eliza Hall Institute of Medical Research, 1G Royal Parade, = Parkville,=20 3050, Victoria, Australia2 Zenyth=20 Therapeutics, 576 Swan Street, Richmond, 3121, Victoria,=20 Australia

Correspondence:
Jeffrey J. Babon
Ph: = +61-3-93452451;=20 Fax: +61-3-93470852
babon@wehi.edu.au

Article Options
= Table=20 of Contents Full=20 Text PDF=20 (757K) Supplemen= tal=20 Data
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Jef= frey=20 J. Babon Ra= ymond=20 S. Norton
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Summary
SOCS3 is essential for regulating = the extent,=20 duration, and specificity of cellular responses to cytokines such = as G-CSF=20 and IL-6. Here we describe the solution structure of SOCS3, the = first=20 structure determined for any SOCS protein, in complex with a=20 phosphotyrosine-containing peptide from the IL-6 receptor = signaling=20 subunit gp130. The structure of the complex shows that seven = peptide=20 residues form a predominantly hydrophobic binding motif. Regions = outside=20 the SOCS3 SH2 domain are important for ligand binding, in = particular, a=20 single 15 residue =CE=B1 helix immediately N-terminal to the SH2 = domain makes=20 direct contacts with the phosphotyrosine binding loop and, in = part,=20 determines its geometry. The SH2 domain itself is remarkable in = that it=20 contains a 35 residue unstructured PEST motif insertion that is = not=20 required for STAT inhibition. The PEST motif increases SOCS3 = turnover and=20 affects its degradation pathway, implying that it has an important = regulatory role inside the cell.
Footnotes
3 Present=20 address: School of Biochemistry, University of Melbourne, = Parkville, 3050,=20 Australia.

Cell		Immunity		Neuron		Molecular Cell		Structure
Current=20 Biology		Developmental = Cell		Cancer = Cell		Chemistry &=20 Biology		Cell=20 Metabolism

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Or should it be blank? 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Article

The Structure of SOCS3 = Reveals the=20 Basis of the Extended SH2 Domain Function and Identifies an = Unstructured=20 Insertion That Regulates Stability

Jeffrey=20 J. Babon,1, Edward=20 J. McManus,1=20 Shenggen Yao,1=20 David=20 P. DeSouza,1,3=20 Lisa=20 A. Mielke,1=20 Naomi=20 S. Sprigg,1=20 Tracy=20 A. Willson,1=20 Douglas=20 J. Hilton,1=20 Nicos=20 A. Nicola,1=20 Manuel Baca,2=20 Sandra=20 E. Nicholson,1=20 and Raymond=20 S. Norton1=20