This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ywp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ywp.gif|left|200px]]<br /><applet load="1ywp" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ywp.gif|left|200px]]
-
caption="1ywp, resolution 1.60&Aring;" />
+
 
-
'''Phospholipase Cgamma1 SH3'''<br />
+
{{Structure
 +
|PDB= 1ywp |SIZE=350|CAPTION= <scene name='initialview01'>1ywp</scene>, resolution 1.60&Aring;
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11]
 +
|GENE= Plcg1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
 +
}}
 +
 
 +
'''Phospholipase Cgamma1 SH3'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1YWP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YWP OCA].
+
1YWP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YWP OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16061254 16061254]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/16061254 16061254]
[[Category: Phosphoinositide phospholipase C]]
[[Category: Phosphoinositide phospholipase C]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
Line 24: Line 33:
[[Category: slp-76]]
[[Category: slp-76]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:50 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:28:27 2008''

Revision as of 13:28, 20 March 2008


PDB ID 1ywp

Drag the structure with the mouse to rotate
, resolution 1.60Å
Gene: Plcg1 (Rattus norvegicus)
Activity: Phosphoinositide phospholipase C, with EC number 3.1.4.11
Coordinates: save as pdb, mmCIF, xml



Phospholipase Cgamma1 SH3


Overview

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.

About this Structure

1YWP is a Single protein structure of sequence from 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 Thu Mar 20 15:28:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools