1gpl
From Proteopedia
(New page: 200px<br /> <applet load="1gpl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gpl, resolution 2.01Å" /> '''RP2 LIPASE'''<br />...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1GPL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Cavia_porcellus Cavia porcellus]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GPL OCA]]. | + | 1GPL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Cavia_porcellus Cavia porcellus]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3]]. Structure known Active Site: CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GPL OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: Cavia porcellus]] | [[Category: Cavia porcellus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Triacylglycerol lipase]] | ||
[[Category: Cambillau, C.]] | [[Category: Cambillau, C.]] | ||
[[Category: Withers-Martinez, C.]] | [[Category: Withers-Martinez, C.]] | ||
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[[Category: serine esterase]] | [[Category: serine esterase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:47:00 2007'' |
Revision as of 10:42, 30 October 2007
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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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