2001
DOI: 10.1006/jmbi.2001.4890
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Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for map kinase regulation 1 1Edited by D. Rees

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Cited by 20 publications
(38 citation statements)
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“…Many of these invariant residues are important for either catalysis and/or structural integrity (25), and they are unlikely to confer PTP substrate specificity. In addition, the crystal structure of the catalytic domain of PTP-SL encompassing residues 254 -549, which correspond to residues 44 -338 in HePTP, highly resembles those of other PTPs (30). Given the overall structural similarities of the PTP-SL catalytic domain to other PTPs, it is uncertain what are the molecular determinants for specific ERK2 dephosphorylation by this group of PTPs.…”
Section: Resultsmentioning
confidence: 99%
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“…Many of these invariant residues are important for either catalysis and/or structural integrity (25), and they are unlikely to confer PTP substrate specificity. In addition, the crystal structure of the catalytic domain of PTP-SL encompassing residues 254 -549, which correspond to residues 44 -338 in HePTP, highly resembles those of other PTPs (30). Given the overall structural similarities of the PTP-SL catalytic domain to other PTPs, it is uncertain what are the molecular determinants for specific ERK2 dephosphorylation by this group of PTPs.…”
Section: Resultsmentioning
confidence: 99%
“…A unique property of the HePTP subfamily of PTPs is the existence of a kinase interaction motif (KIM, residues 17-30 in HePTP) NH 2 -terminal to the catalytic domain that is directly involved in ERK2 binding (17,19,22). Because the crystal structure of PTP-SL does not include the KIM sequence (30), it is unclear how KIM contributes to the specificity of HePTP toward ERK2. Finally, it is also not known how HePTP avoids nonspecific dephosphorylation of Tyr(P)-containing proteins other than ERK2.…”
Section: Resultsmentioning
confidence: 99%
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“…The HePTP catalytic domain, like those of the other KIM PTPs, has a structure that is somewhat distinct from other classical PTPs [46,49]. The KIM motif, which is not present in canonical PTPs, such as PTP1B, forms an α-helix (α0) at the Nterminal portion of the KIM PTP catalytic domain; also, there are substantial backbonestructure deviations between the KIM PTP and PTP1B catalytic domains [50]. More relevantly, the positioning of I219 in the PTP1B active site differs substantially from that of I274 in HePTP ( Figure 6): PTP1B's I219 side chain comprises a large part of the "tunnel" surface leading to the enzyme's active-site cysteine ( Figure 6A), whereas HePTP's I274 side chain is mostly buried and does not make up a significant part of the active site's surface ( Figure 6B).…”
Section: Heptpmentioning
confidence: 99%