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| - | [[Image:1ywo.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1ywo.png|left|200px]] |
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| | {{STRUCTURE_1ywo| PDB=1ywo | SCENE= }} | | {{STRUCTURE_1ywo| PDB=1ywo | SCENE= }} |
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| - | '''Phospholipase Cgamma1 SH3 in complex with a SLP-76 motif'''
| + | ===Phospholipase Cgamma1 SH3 in complex with a SLP-76 motif=== |
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| - | ==Overview==
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| - | The enzyme phospholipase Cgamma1 (PLCgamma1) is essential for T cell signaling and activation. Following T cell receptor ligation, PLCgamma1 interacts through its SH2 and SH3 domains with the adaptors LAT and SLP-76, respectively, to form a multiprotein signaling complex that leads to activation of PLCgamma1 by Syk tyrosine kinases. To identify the binding site for PLCgamma1 in SLP-76, we used isothermal titration calorimetry to measure affinities for the interaction of PLCgamma1-SH3 with a set of overlapping peptides spanning the central proline-rich region of SLP-76. PLCgamma1-SH3 bound with high specificity to the SLP-76 motif 186PPVPPQRP193, which represents the minimal binding site. To understand the basis for selective recognition, we determined the crystal structures of PLCgamma1-SH3 in free form, and bound to a 10-mer peptide containing this site, to resolutions of 1.60 A and 1.81 A, respectively. The structures reveal that several key contacting residues of the SH3 shift toward the SLP-76 peptide upon complex formation, optimizing the fit and strengthening hydrophobic interactions. Selectivity results mainly from strict shape complementarity between protein and peptide, rather than sequence-specific hydrogen bonding. In addition, Pro193 of SLP-76 assists in positioning Arg192 into the compass pocket of PLCgamma1-SH3, which coordinates the compass residue through an unusual aspartate. The PLCgamma1-SH3/SLP-76 structure provides insights into ligand binding by SH3 domains related to PLCgamma1-SH3, as well as into recognition by PLCgamma1 of signaling partners other than SLP-76. | + | The line below this paragraph, {{ABSTRACT_PUBMED_16061254}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16061254 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16061254}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Sh3]] | | [[Category: Sh3]] |
| | [[Category: Slp-76]] | | [[Category: Slp-76]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:53:24 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:30:18 2008'' |
Revision as of 20:30, 28 July 2008
Template:STRUCTURE 1ywo
Phospholipase Cgamma1 SH3 in complex with a SLP-76 motif
Template:ABSTRACT PUBMED 16061254
About this Structure
1YWO is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structural basis for recognition of the T cell adaptor protein SLP-76 by the SH3 domain of phospholipase Cgamma1., Deng L, Velikovsky CA, Swaminathan CP, Cho S, Mariuzza RA, J Mol Biol. 2005 Sep 9;352(1):1-10. PMID:16061254
Page seeded by OCA on Mon Jul 28 23:30:18 2008
