1bm6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1bm6.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1bm6.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bm6| PDB=1bm6 | SCENE= }}
{{STRUCTURE_1bm6| PDB=1bm6 | SCENE= }}
-
'''SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 COMPLEXED TO A POTENT NON-PEPTIDIC INHIBITOR, NMR, 20 STRUCTURES'''
+
===SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 COMPLEXED TO A POTENT NON-PEPTIDIC INHIBITOR, NMR, 20 STRUCTURES===
-
==Overview==
+
<!--
-
The full three-dimensional structure of the catalytic domain of human stromelysin-1 (SCD) complexed to a novel and potent, nonpeptidic inhibitor has been determined by nuclear magnetic resonance spectroscopy (NMR). To accurately mimic assay conditions, the structure was obtained in Tris buffer at pH 6.8 and without the presence of organic solvent. The results showed that the major site of enzyme-inhibitor interaction occurs in the S1' pocket whereas portions of the inhibitor that occupy the shallow S2' and S1 pockets remained primarily solvent exposed. Because this relatively small inhibitor could not deeply penetrate stromelysin's long narrow hydrophobic S1' pocket, the enzyme was found to adopt a dramatic fold in the loop region spanning residues 221-231, allowing occupation of the solvent-accessible S1' channel by the enzyme itself. This remarkable conformational fold at the enzyme binding site resulted in constriction of the S1' loop region about the inhibitor. Examination of the tertiary structure of the stromelysin-inhibitor complex revealed few hydrogen-bonding or hydrophobic interactions between the inhibitor and enzyme that can contribute to overall binding energy; hence the resultant compact structure may in part account for the relatively high potency exhibited by this inhibitor.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9760240}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9760240 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9760240}}
==About this Structure==
==About this Structure==
-
1BM6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM6 OCA].
+
1BM6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM6 OCA].
==Reference==
==Reference==
Line 31: Line 35:
[[Category: Metalloprotease]]
[[Category: Metalloprotease]]
[[Category: Metzincin]]
[[Category: Metzincin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:41:31 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:22:25 2008''

Revision as of 16:22, 30 June 2008

Image:1bm6.png

Template:STRUCTURE 1bm6

SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 COMPLEXED TO A POTENT NON-PEPTIDIC INHIBITOR, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 9760240

About this Structure

1BM6 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Solution structure of the catalytic domain of human stromelysin-1 complexed to a potent, nonpeptidic inhibitor., Li YC, Zhang X, Melton R, Ganu V, Gonnella NC, Biochemistry. 1998 Oct 6;37(40):14048-56. PMID:9760240

Page seeded by OCA on Mon Jun 30 19:22:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bm6"
Personal tools