1hug

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hug.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1hug.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hug| PDB=1hug | SCENE= }}
{{STRUCTURE_1hug| PDB=1hug | SCENE= }}
-
'''DIFFERENCES IN ANIONIC INHIBITION OF HUMAN CARBONIC ANHYDRASE I REVEALED FROM THE STRUCTURES OF IODIDE AND GOLD CYANIDE INHIBITOR COMPLEXES'''
+
===DIFFERENCES IN ANIONIC INHIBITION OF HUMAN CARBONIC ANHYDRASE I REVEALED FROM THE STRUCTURES OF IODIDE AND GOLD CYANIDE INHIBITOR COMPLEXES===
-
==Overview==
+
<!--
-
The crystal structures of two anionic inhibitor complexes of human carbonic anhydrase I (HCAI), namely, HCAI-iodide and HCAI-Au(CN)(2)(-), have been refined by the restrained least-squares method at 2.2 and 2 A nominal resolution, respectively, with good stereochemistry for the final models. The R values have improved from 30.3 to 16.6% for HCAI-iodide and from 28.8 to 17.1% for HCAI-Au(CN)(2)(-). The sites of inhibitor binding as elucidated are totally different in the two structures. The iodide anion replaces the zinc-bound H(2)O/OH(-) ligand and renders the enzyme inactive. This result confirms that the zinc-bound H(2)O/OH(-) is the activity-linked group in carbonic anhydrase enzymes. Au(CN)(2)(-) binds at a different and new site near the zinc ion, without liganding to the metal. The N atom of Au(CN)(2)(-) is within hydrogen-bonding distance of the zinc-bound H(2)O/OH(-) group which shifts by about 0.4 A away from the zinc ion in relation to its position in the native HCAI. It is proposed that the presence of the inhibitor Au(CN)(2)(-) results in a conformational reorientation of the activity-linked group, due to hydrogen-bond formation with the inhibitor, which in turn sterically hinders the binding of the substrate CO(2) molecule in the active site, leading to the inhibition of HCAI enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15299369}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15299369 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15299369}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Kannan, K K.]]
[[Category: Kannan, K K.]]
[[Category: Kumar, V.]]
[[Category: Kumar, V.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:14:33 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:42:18 2008''

Revision as of 05:42, 1 July 2008

Image:1hug.png

Template:STRUCTURE 1hug

DIFFERENCES IN ANIONIC INHIBITION OF HUMAN CARBONIC ANHYDRASE I REVEALED FROM THE STRUCTURES OF IODIDE AND GOLD CYANIDE INHIBITOR COMPLEXES

Template:ABSTRACT PUBMED 15299369

About this Structure

1HUG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Differences in anionic inhibition of human carbonic anhydrase I revealed from the structures of iodide and gold cyanide inhibitor complexes., Kumar V, Kannan KK, Sathyamurthi P, Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):731-8. PMID:15299369

Page seeded by OCA on Tue Jul 1 08:42:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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