Ontology type: schema:ScholarlyArticle
1994-04
AUTHORSMichael J. Eck, Shane K. Atwell, Steven E. Shoelson, Stephen C. Harrison
ABSTRACTTHE kinase p56lck (Lck) is a T-lymphocyte-specific member of the Src family of non-receptor tyrosine kinases1. Members of the Src family each contain unique amino-terminal regions, followed by Src-homology domains SH3 and SH2, and a tyrosine kinase domain. SH3 and SH2 domains mediate critical protein interactions in many signal-transducing pathways2. They are small, independently folded modules of about 60 and 100 residues, respectively, and they are often but not always found together in the same molecule. Like all nine Src-family kinases (reviewed in ref. 3), Lck is regulated by phosphorylation of a tyrosine in the short C-terminal tail of its catalytic domain4. There is evidence that binding of the phosphorylated tail to the SH2 domain inhibits catalytic activity of the kinase domain5,6 and that the SH3 and SH2 domains may act together to effect this regulation7. Here we report the crystal structures for a fragment of Lck bearing its SH3 and SH2 domains, alone and in complex with a phosphotyrosyl peptide containing the sequence of the Lck C-terminal regulatory tail. The latter complex represents the regulatory apparatus of Lck. The SH3–SH2 fragment forms similar dimers in both crystals, and the tail peptide binds at the intermolecular SH3/SH2 contact. The two structures show how an SH3 domain might recognize a specific target and suggest how dimerization could play a role in regulating Src-family kinases. More... »
PAGES764-769
http://scigraph.springernature.com/pub.10.1038/368764a0
DOIhttp://dx.doi.org/10.1038/368764a0
DIMENSIONShttps://app.dimensions.ai/details/publication/pub.1026759430
PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/7512222
JSON-LD is the canonical representation for SciGraph data.
TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT
[
{
"@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json",
"about": [
{
"id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/06",
"inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/",
"name": "Biological Sciences",
"type": "DefinedTerm"
},
{
"id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0601",
"inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/",
"name": "Biochemistry and Cell Biology",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Amino Acid Sequence",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Binding Sites",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Computer Graphics",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Crystallography, X-Ray",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Lymphocyte Specific Protein Tyrosine Kinase p56(lck)",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Models, Molecular",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Molecular Sequence Data",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Phosphopeptides",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Phosphorylation",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Protein Conformation",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Protein Structure, Secondary",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Protein-Tyrosine Kinases",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Proto-Oncogene Proteins pp60(c-src)",
"type": "DefinedTerm"
}
],
"author": [
{
"affiliation": {
"alternateName": "Department of Microbiology and Molecular Genetics, Harvard Medical School, 02115, Boston, Massachusetts, USA",
"id": "http://www.grid.ac/institutes/grid.38142.3c",
"name": [
"Howard Hughes Medical Institute and Laboratory of Molecular Medicine, Children's Hospital, 300 Longwood Avenue, 02115, Boston, Massachusetts, USA",
"Department of Microbiology and Molecular Genetics, Harvard Medical School, 02115, Boston, Massachusetts, USA"
],
"type": "Organization"
},
"familyName": "Eck",
"givenName": "Michael J.",
"id": "sg:person.01212245744.44",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01212245744.44"
],
"type": "Person"
},
{
"affiliation": {
"alternateName": "Howard Hughes Medical Institute and Laboratory of Molecular Medicine, Children's Hospital, 300 Longwood Avenue, 02115, Boston, Massachusetts, USA",
"id": "http://www.grid.ac/institutes/grid.2515.3",
"name": [
"Howard Hughes Medical Institute and Laboratory of Molecular Medicine, Children's Hospital, 300 Longwood Avenue, 02115, Boston, Massachusetts, USA"
],
"type": "Organization"
},
"familyName": "Atwell",
"givenName": "Shane K.",
"type": "Person"
},
{
"affiliation": {
"alternateName": "Research Division, Joslin Diabetes Center, Department of Medicine, Brigham & Women's Hospital, Harvard Medical School, 02115, Boston, Massachusetts, USA",
"id": "http://www.grid.ac/institutes/grid.38142.3c",
"name": [
"Research Division, Joslin Diabetes Center, Department of Medicine, Brigham & Women's Hospital, Harvard Medical School, 02115, Boston, Massachusetts, USA"
],
"type": "Organization"
},
"familyName": "Shoelson",
"givenName": "Steven E.",
"id": "sg:person.01021130270.20",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01021130270.20"
],
"type": "Person"
},
{
"affiliation": {
"alternateName": "Department of Biochemistry & Molecular Biology, Harvard University, 02138, Cambridge, Massachusetts, USA",
"id": "http://www.grid.ac/institutes/grid.38142.3c",
"name": [
"Howard Hughes Medical Institute and Laboratory of Molecular Medicine, Children's Hospital, 300 Longwood Avenue, 02115, Boston, Massachusetts, USA",
"Department of Biochemistry & Molecular Biology, Harvard University, 02138, Cambridge, Massachusetts, USA"
],
"type": "Organization"
},
"familyName": "Harrison",
"givenName": "Stephen C.",
"id": "sg:person.013635370377.53",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.013635370377.53"
],
"type": "Person"
}
],
"citation": [
{
"id": "sg:pub.10.1038/358684a0",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1045636554",
"https://doi.org/10.1038/358684a0"
],
"type": "CreativeWork"
},
{
"id": "sg:pub.10.1038/362087a0",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1001978864",
"https://doi.org/10.1038/362087a0"
],
"type": "CreativeWork"
},
{
"id": "sg:pub.10.1038/350062a0",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1001221915",
"https://doi.org/10.1038/350062a0"
],
"type": "CreativeWork"
},
{
"id": "sg:pub.10.1038/359851a0",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1051712088",
"https://doi.org/10.1038/359851a0"
],
"type": "CreativeWork"
},
{
"id": "sg:pub.10.1038/358646a0",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1021461565",
"https://doi.org/10.1038/358646a0"
],
"type": "CreativeWork"
}
],
"datePublished": "1994-04",
"datePublishedReg": "1994-04-01",
"description": "THE kinase p56lck (Lck) is a T-lymphocyte-specific member of the Src family of non-receptor tyrosine kinases1. Members of the Src family each contain unique amino-terminal regions, followed by Src-homology domains SH3 and SH2, and a tyrosine kinase domain. SH3 and SH2 domains mediate critical protein interactions in many signal-transducing pathways2. They are small, independently folded modules of about 60 and 100 residues, respectively, and they are often but not always found together in the same molecule. Like all nine Src-family kinases (reviewed in ref. 3), Lck is regulated by phosphorylation of a tyrosine in the short C-terminal tail of its catalytic domain4. There is evidence that binding of the phosphorylated tail to the SH2 domain inhibits catalytic activity of the kinase domain5,6 and that the SH3 and SH2 domains may act together to effect this regulation7. Here we report the crystal structures for a fragment of Lck bearing its SH3 and SH2 domains, alone and in complex with a phosphotyrosyl peptide containing the sequence of the Lck C-terminal regulatory tail. The latter complex represents the regulatory apparatus of Lck. The SH3\u2013SH2 fragment forms similar dimers in both crystals, and the tail peptide binds at the intermolecular SH3/SH2 contact. The two structures show how an SH3 domain might recognize a specific target and suggest how dimerization could play a role in regulating Src-family kinases.",
"genre": "article",
"id": "sg:pub.10.1038/368764a0",
"isAccessibleForFree": false,
"isPartOf": [
{
"id": "sg:journal.1018957",
"issn": [
"0028-0836",
"1476-4687"
],
"name": "Nature",
"publisher": "Springer Nature",
"type": "Periodical"
},
{
"issueNumber": "6473",
"type": "PublicationIssue"
},
{
"type": "PublicationVolume",
"volumeNumber": "368"
}
],
"keywords": [
"Src family kinases",
"SH2 domain",
"Src family",
"Src family tyrosine kinase Lck",
"unique amino-terminal region",
"tyrosine kinase Lck",
"critical protein interactions",
"amino-terminal region",
"tyrosine kinase domain",
"phosphorylated tail",
"regulatory tail",
"Src homology",
"kinase Lck",
"SH3 domain",
"regulatory domain",
"kinase domain",
"protein interactions",
"terminal tail",
"phosphotyrosyl peptides",
"kinase p56lck",
"SH3",
"Lck",
"SH2",
"regulatory apparatus",
"kinase",
"peptide binds",
"specific targets",
"domain",
"tail",
"similar dimers",
"p56lck",
"family",
"phosphorylation",
"complexes",
"members",
"binds",
"crystal structure",
"residues",
"same molecule",
"tyrosine",
"dimerization",
"binding",
"sequence",
"fragments",
"catalytic activity",
"peptides",
"latter complex",
"dimers",
"target",
"molecules",
"structure",
"role",
"interaction",
"activity",
"region",
"apparatus",
"evidence",
"contact",
"module",
"crystals"
],
"name": "Structure of the regulatory domains of the Src-family tyrosine kinase Lck",
"pagination": "764-769",
"productId": [
{
"name": "dimensions_id",
"type": "PropertyValue",
"value": [
"pub.1026759430"
]
},
{
"name": "doi",
"type": "PropertyValue",
"value": [
"10.1038/368764a0"
]
},
{
"name": "pubmed_id",
"type": "PropertyValue",
"value": [
"7512222"
]
}
],
"sameAs": [
"https://doi.org/10.1038/368764a0",
"https://app.dimensions.ai/details/publication/pub.1026759430"
],
"sdDataset": "articles",
"sdDatePublished": "2022-08-04T16:52",
"sdLicense": "https://scigraph.springernature.com/explorer/license/",
"sdPublisher": {
"name": "Springer Nature - SN SciGraph project",
"type": "Organization"
},
"sdSource": "s3://com-springernature-scigraph/baseset/20220804/entities/gbq_results/article/article_247.jsonl",
"type": "ScholarlyArticle",
"url": "https://doi.org/10.1038/368764a0"
}
]Download the RDF metadata as: json-ld nt turtle xml License info
JSON-LD is a popular format for linked data which is fully compatible with JSON.
curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1038/368764a0'
N-Triples is a line-based linked data format ideal for batch operations.
curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1038/368764a0'
Turtle is a human-readable linked data format.
curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/368764a0'
RDF/XML is a standard XML format for linked data.
curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/368764a0'
This table displays all metadata directly associated to this object as RDF triples.
221 TRIPLES
21 PREDICATES
104 URIs
91 LITERALS
20 BLANK NODES