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J Biol Chem, Vol. 275, Issue 6, 4066-4071, February 11, 2000
From the The substrate specificity of the catalytic domain
of SHP-1, an important regulator in the proliferation and development
of hematopoietic cells, is critical for understanding the physiological functions of SHP-1. Here we report the crystal structures of the catalytic domain of SHP-1 complexed with two peptide substrates derived
from SIRP
Structural Basis for Substrate Specificity of Protein-tyrosine
Phosphatase SHP-1*
§,,,,
Program in Molecular Medicine, University of
Massachusetts Medical School, Worcester, Massachusetts 01605 and the
¶ Department of Medicine, Vanderbilt University,
Nashville, Tennessee 37232
, a member of the signal-regulatory proteins. We show that
the variable 
5-loop-6 motif confers SHP-1 substrate specificity
at the P-4 and further N-terminal subpockets. We also observe a novel
residue shift at P-2, the highly conserved subpocket in protein-
tyrosine phosphatases. Our observations provide new insight into the
substrate specificity of SHP-1.
*
This work was supported by a Career Development Award from
the American Diabetes Association (to G. W. Z.), the Pilot
project from the DERC Program of the University of Massachusetts
Medical School (to G. W. Z.), and National Institutes of
Health Grants AL45858 (to G. W. Z.) and HL57393 (to Z. J. Z.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
508-856-6869; Fax: 508-856-4289; E-mail: G.Zhou@ummed.edu.
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