3U0V: Crystal Structure Analysis Of Human Lyplal1

Citation:
Abstract
Sequence homology indicates the existence of three human cytosolic acyl protein thioesterases, including APT1 that is known to depalmitoylate H- and N-Ras. One of them is the lysophospholipase-like 1 (LYPLAL1) protein that on the one hand is predicted to be closely related to APT1 but on the other hand might also function as a potential triacylglycerol lipase involved in obesity. However, its role remained unclear. The 1.7 A crystal structure of LYPLAL1 reveals a fold very similar to APT1, as expected, but features a shape of the active site that precludes binding of long-chain substrates. Biochemical data demonstrate that LYPLAL1 exhibits neither phospholipase nor triacylglycerol lipase activity, but rather accepts short-chain substrates. Furthermore, extensive screening efforts using chemical array technique revealed a first small molecule inhibitor of LYPLAL1.
PDB ID: 3U0VDownload
MMDB ID: 95092
PDB Deposition Date: 2011/9/29
Updated in MMDB: 2011/11
Experimental Method:
x-ray diffraction
Resolution: 1.72  Å
Source Organism:
Similar Structures:
Biological Unit for 3U0V: monomeric; determined by author and by software (PISA)
Molecular Components in 3U0V
Label Count Molecule
Protein (1 molecule)
1
Lysophospholipase-like Protein 1(Gene symbol: LYPLAL1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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