1ckb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1ckb.jpg|left|200px]]
[[Image:1ckb.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1ckb |SIZE=350|CAPTION= <scene name='initialview01'>1ckb</scene>, resolution 1.90&Aring;
+
The line below this paragraph, containing "STRUCTURE_1ckb", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND=
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE= PCR PRODUCT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1ckb| PDB=1ckb | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ckb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ckb OCA], [http://www.ebi.ac.uk/pdbsum/1ckb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ckb RCSB]</span>
+
-
}}
+
'''STRUCTURAL BASIS FOR THE SPECIFIC INTERACTION OF LYSINE-CONTAINING PROLINE-RICH PEPTIDES WITH THE N-TERMINAL SH3 DOMAIN OF C-CRK'''
'''STRUCTURAL BASIS FOR THE SPECIFIC INTERACTION OF LYSINE-CONTAINING PROLINE-RICH PEPTIDES WITH THE N-TERMINAL SH3 DOMAIN OF C-CRK'''
Line 28: Line 25:
[[Category: Kuriyan, J.]]
[[Category: Kuriyan, J.]]
[[Category: Wu, X.]]
[[Category: Wu, X.]]
-
[[Category: complex (oncogene protein/peptide)]]
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:49:29 2008''
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:23:15 2008''
+

Revision as of 09:49, 2 May 2008

Template:STRUCTURE 1ckb

STRUCTURAL BASIS FOR THE SPECIFIC INTERACTION OF LYSINE-CONTAINING PROLINE-RICH PEPTIDES WITH THE N-TERMINAL SH3 DOMAIN OF C-CRK


Overview

BACKGROUND: Proline-rich segments in the guanine nucleotide exchange factor C3G bind much more strongly to the N-terminal Src homology 3 domain (SH3-N) of the proto-oncogene product c-Crk than to other SH3 domains. The presence of a lysine instead of an arginine in the peptides derived from C3G appears to be crucial for this specificity towards c-Crk. RESULTS: In order to understand the chemical basis of this specificity we have determined the crystal structure of Crk SH3-N in complex with a high affinity peptide from C3G (PPPALPPKKR, Kd approximately 2 microM) at 1.5 A resolution. The peptide adopts a polyproline type II helix that binds, as dictated by electrostatic complementarity, in reversed orientation relative to the orientation seen in the earliest structures of SH3-peptide complexes. A lysine in the C3G peptide is tightly coordinated by three acidic residues in the SH3 domain. In contrast, the co-crystal structure of c-Crk SH3-N and a peptide containing an arginine at the equivalent position (determined at 1.9 A resolution) reveals non-optimal geometry for the arginine and increased disorder. CONCLUSIONS: The c-Crk SH3 domain engages in an unusual lysine-specific interaction that is rarely seen in protein structures, and which appears to be a key determinant of its unique ability to bind the C3G peptides with high affinity.

About this Structure

1CKB is a Single protein structure of sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk., Wu X, Knudsen B, Feller SM, Zheng J, Sali A, Cowburn D, Hanafusa H, Kuriyan J, Structure. 1995 Feb 15;3(2):215-26. PMID:7735837 Page seeded by OCA on Fri May 2 12:49:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools