2PLD: NUCLEAR MAGNETIC RESONANCE STRUCTURE OF AN SH2 DOMAIN OF PHOSPHOLIPASE C-GAMMA1 COMPLEXED WITH A HIGH AFFINITY BINDING PEPTIDE

Citation:
Abstract
The solution structure of the C-terminal SH2 domain of phospholipase C-gamma 1 (PLC-gamma 1), in complex with a phosphopeptide corresponding to its Tyr-1021 high affinity binding site on the platelet-derived growth factor receptor, has been determined by nuclear magnetic resonance spectroscopy. The topology of the SH2-phosphopeptide complex is similar to previously reported Src and Lck SH2 complexes. However, the binding site for residues C-terminal to the phosphotyrosine (pTyr) is an extended groove that contacts peptide residues at the +1 to +6 positions relative to the pTyr. This striking difference from Src and Lck reflects the fact that the PLC-gamma 1 complex involves binding of a phosphopeptide with predominantly hydrophobic residues C-terminal to the pTyr and therefore serves as a prototype for a second class of SH2-phosphopeptide interactions.
PDB ID: 2PLDDownload
MMDB ID: 2866
PDB Deposition Date: 1994/8/19
Updated in MMDB: 2017/12
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2PLD: dimeric; determined by author
Molecular Components in 2PLD
Label Count Molecule
Proteins (2 molecules)
1
Phospholipase C Gamma-1, C-terminal SH2 Domain(Gene symbol: PLCG1)
Molecule annotation
1
Phosphopeptide From Pdgf(Gene symbol: PDGFRB)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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