1gpl
From Proteopedia
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RP2 LIPASE
Overview
We designed chimeric mutants by exchanging the lid domains of the, classical human pancreatic lipase (HPL) and the guinea pig pancreatic, lipase related protein 2 (GPLRP2). This latter enzyme possesses naturally, a large deletion within the lid domain and is not activated by lipid/water, interfaces. Furthermore, GPLRP2 exhibits phospholipase A1 and lipase, activities in the same order of magnitude, whereas HPL has no significant, phospholipase activity and displays a clear interfacial activation. An HPL, mutant [HPL(-lid)] with GPLRP2 mini-lid domain does not display, interfacial activation. Its specific activity toward triglycerides is, however, dramatically reduced. A GPLRP2 mutant [GPLRP2(+lid)] with HPL, full-length lid domain is not interfacially activated, and its lid domain, ... [(full description)]
About this Structure
1GPL is a [Single protein] structure of sequence from [Cavia porcellus] with CA as [ligand]. Active as [Triacylglycerol lipase], with EC number [3.1.1.3]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
Reference
Pancreatic lipase structure-function relationships by domain exchange., Carriere F, Thirstrup K, Hjorth S, Ferrato F, Nielsen PF, Withers-Martinez C, Cambillau C, Boel E, Thim L, Verger R, Biochemistry. 1997 Jan 7;36(1):239-48. PMID:8993339
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