| http://purl.uniprot.org/citations/17468108 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17468108 | http://www.w3.org/2000/01/rdf-schema#comment | "The leukocyte beta2 integrins are heterodimeric adhesion receptors required for a functional immune system. Many leukocyte adhesion deficiency-1 (LAD-1) mutations disrupt the expression and function of beta2 integrins. Herein, we further characterized the LAD-1 mutation N329S in the beta2 inserted (I)-like domain. This mutation converted alphaLbeta2 from a resting into a high affinity conformer because alphaLbeta2N329S transfectants adhered avidly to ligand intercellular adhesion molecule (ICAM)-3 in the absence of additional activating agent. An extended open conformation is adopted by alphaLbeta2N329S because of its reactivity with the beta2 activation reporter monoclonal antibodies MEM148 and KIM127. A corresponding mutation in beta3 generated constitutively active alphaIIbbeta3 that adhered to fibrinogen. This Asn is conserved in all human beta subunits, and it resides before the last helix of the I-like domain, which is known to be important in activation signal propagation. By mutagenesis studies and review of existing integrin structures, we conjectured that this conserved Asn may have a primary role in shaping the I-like domain by stabilizing the conformation of the alpha7 helix and the beta6-alpha7 loop in the I-like domain."xsd:string |
| http://purl.uniprot.org/citations/17468108 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m701386200"xsd:string |
| http://purl.uniprot.org/citations/17468108 | http://purl.uniprot.org/core/author | "Cheng M."xsd:string |
| http://purl.uniprot.org/citations/17468108 | http://purl.uniprot.org/core/author | "Tang R.H."xsd:string |
| http://purl.uniprot.org/citations/17468108 | http://purl.uniprot.org/core/author | "Law S.K.A."xsd:string |
| http://purl.uniprot.org/citations/17468108 | http://purl.uniprot.org/core/author | "Tan S.M."xsd:string |
| http://purl.uniprot.org/citations/17468108 | http://purl.uniprot.org/core/author | "Shi M.L."xsd:string |
| http://purl.uniprot.org/citations/17468108 | http://purl.uniprot.org/core/author | "Foo S.Y."xsd:string |
| http://purl.uniprot.org/citations/17468108 | http://purl.uniprot.org/core/author | "Kong L.S."xsd:string |
| http://purl.uniprot.org/citations/17468108 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17468108 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/17468108 | http://purl.uniprot.org/core/pages | "18225-18232"xsd:string |
| http://purl.uniprot.org/citations/17468108 | http://purl.uniprot.org/core/title | "Mutation of a conserved asparagine in the I-like domain promotes constitutively active integrins alphaLbeta2 and alphaIIbbeta3."xsd:string |
| http://purl.uniprot.org/citations/17468108 | http://purl.uniprot.org/core/volume | "282"xsd:string |
| http://purl.uniprot.org/citations/17468108 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17468108 |
| http://purl.uniprot.org/citations/17468108 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17468108 |
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| http://purl.uniprot.org/uniprot/#_A0A024DBF0-mappedCitation-17468108 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17468108 |