This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1k8q

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1k8q.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1k8q.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1k8q| PDB=1k8q | SCENE= }}
{{STRUCTURE_1k8q| PDB=1k8q | SCENE= }}
-
'''CRYSTAL STRUCTURE OF DOG GASTRIC LIPASE IN COMPLEX WITH A PHOSPHONATE INHIBITOR'''
+
===CRYSTAL STRUCTURE OF DOG GASTRIC LIPASE IN COMPLEX WITH A PHOSPHONATE INHIBITOR===
-
==Overview==
+
<!--
-
Fat digestion in humans and some mammals such as dogs requires the successive intervention of two lipases: gastric lipase, which is stable and active despite the highly acidic stomach environment, followed by the classical pancreatic lipase secreted into the duodenum. We previously solved the structure of recombinant human gastric lipase (HGL) at 3.0-A resolution in its closed form; this was the first structure to be described within the mammalian acid lipase family. Here we report on the open structure of the recombinant dog gastric lipase (r-DGL) at 2.7-A resolution in complex with the undecyl-butyl (C11Y4) phosphonate inhibitor. HGL and r-DGL show 85.7% amino acid sequence identity, which makes it relevant to compare the forms from two different species. The open r-DGL structure confirms the previous description of the HGL catalytic triad (Ser(153), His(353), and Asp(324)) with the catalytic serine buried and an oxyanion hole (NH groups of Gln(154) and Leu(67)). In r-DGL, the binding of the C11Y4 phosphonate inhibitor induces part of the cap domain, the lid, to roll over the enzyme surface and to expose a catalytic crevice measuring approximately 20 x 20 x 7 A(3). The C11Y4 phosphonate fits into this crevice, and a molecule of beta-octyl glucoside fills up the crevice. The C11Y4 phosphonate inhibitor and the detergent molecule suggest a possible binding mode for the natural substrates, the triglyceride molecules.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11689574}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11689574 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11689574}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Verger, R.]]
[[Category: Verger, R.]]
[[Category: Apha beta hydrolase fold]]
[[Category: Apha beta hydrolase fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:26:36 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 09:57:23 2008''

Revision as of 06:57, 2 July 2008

Image:1k8q.png

Template:STRUCTURE 1k8q

CRYSTAL STRUCTURE OF DOG GASTRIC LIPASE IN COMPLEX WITH A PHOSPHONATE INHIBITOR

Template:ABSTRACT PUBMED 11689574

About this Structure

1K8Q is a Single protein structure of sequence from Canis lupus familiaris. Full crystallographic information is available from OCA.

Reference

Crystal structure of the open form of dog gastric lipase in complex with a phosphonate inhibitor., Roussel A, Miled N, Berti-Dupuis L, Riviere M, Spinelli S, Berna P, Gruber V, Verger R, Cambillau C, J Biol Chem. 2002 Jan 18;277(3):2266-74. Epub 2001 Oct 31. PMID:11689574

Page seeded by OCA on Wed Jul 2 09:57:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1k8q"
Personal tools