We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1a4m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1a4m.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1a4m.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1a4m| PDB=1a4m | SCENE= }}
{{STRUCTURE_1a4m| PDB=1a4m | SCENE= }}
-
'''ADA STRUCTURE COMPLEXED WITH PURINE RIBOSIDE AT PH 7.0'''
+
===ADA STRUCTURE COMPLEXED WITH PURINE RIBOSIDE AT PH 7.0===
-
==Overview==
+
<!--
-
Adenosine deaminase, which catalyzes the irreversible hydrolytic deamination of adenosine nucleosides to inosine nucleosides and ammonia, is a key enzyme in purine metabolism and lymphoid development. The X-ray structures of murine adenosine deaminase with bound potent inhibitors (Ki values approximately 10(-13) M) (8R)-hydroxyl-2'-deoxycoformycin (pentostatin), a transition state analogue, and (6S)-hydroxyl-1,6-dihydropurine riboside, a reaction coordinate analogue, have been determined and refined to resolutions of 2.6 and 1.95 A, respectively. Crystals of both complexes were obtained at pH 7, where the enzyme is fully active, in an identical space group with the asymmetric unit containing four molecules. In addition to the very high degree of similarity between the four independent molecules in each complex structure, there is also considerable structural similarity of the complex with the dihydropurine riboside with that of an identical complex previously determined at pH 4.2 where the enzyme is 20% active. The interactions between the enzyme and the two analogues are extremely similar. These include the coordination of the 8R- or 6S-hydroxyl group of the analogues to the Zn2+ which mainly contributes to the strong potency and very high degree of stereospecificity of inhibition by these analogues. The interactions are further indicative of the structural and chemical requirements of substrates. These structures and recent site-directed mutagenesis have further shed light on the catalytic mechanism of the enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9622483}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9622483 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9622483}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Purine riboside]]
[[Category: Purine riboside]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:48:18 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:06:54 2008''

Revision as of 13:06, 30 June 2008

Image:1a4m.png

Template:STRUCTURE 1a4m

ADA STRUCTURE COMPLEXED WITH PURINE RIBOSIDE AT PH 7.0

Template:ABSTRACT PUBMED 9622483

About this Structure

1A4M is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity., Wang Z, Quiocho FA, Biochemistry. 1998 Jun 9;37(23):8314-24. PMID:9622483

Page seeded by OCA on Mon Jun 30 16:06:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a4m"
Personal tools