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.


1zzz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zzz.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1zzz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zzz| PDB=1zzz | SCENE= }}
{{STRUCTURE_1zzz| PDB=1zzz | SCENE= }}
-
'''TRYPSIN INHIBITORS WITH RIGID TRIPEPTIDYL ALDEHYDES'''
+
===TRYPSIN INHIBITORS WITH RIGID TRIPEPTIDYL ALDEHYDES===
-
==Overview==
+
<!--
-
The crystal structures of three highly potent and selective low-molecular weight rigid peptidyl aldehyde inhibitors complexed with thrombin have been determined and refined to R values 0.152-0. 170 at 1.8-2.1 A resolution. Since the selectivity of two of the inhibitors was &gt;1600 with respect to trypsin, the structures of trypsin-inhibited complexes of these inhibitors were also determined (R = 0.142-0.157 at 1.9-2.1 A resolution). The selectivity appears to reside in the inability of a benzenesulfonamide group to bind at the equivalent of the D-enantiomorphic S3 site of thrombin, which may be related to the lack of a 60-insertion loop in trypsin. All the inhibitors have a novel lactam moiety at the P3 position, while the two with greatest trypsin selectivity have a guanidinopiperidyl group at the P1 position that binds in the S1 specificity site. Differences in the binding constants of these inhibitors are correlated with their interactions with thrombin and trypsin. The kinetics of inhibition vary from slow to fast with thrombin and are fast in all cases with trypsin. The kinetics are examined in terms of the slow formation of a stable transition-state complex in a two-step mechanism. The structures of both thrombin and trypsin complexes show similar well-defined transition states in the S1 site and at the electrophilic carbon atom and Ser195OG. The trypsin structures, however, suggest that the first step in a two-step kinetic mechanism may involve formation of a weak transition-state complex, rather than binding dominated by the P2-P4 positions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9724521}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9724521 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9724521}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Zhang, E.]]
[[Category: Zhang, E.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:17:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:54:25 2008''

Revision as of 16:54, 27 July 2008

Image:1zzz.png

Template:STRUCTURE 1zzz

TRYPSIN INHIBITORS WITH RIGID TRIPEPTIDYL ALDEHYDES

Template:ABSTRACT PUBMED 9724521

About this Structure

1ZZZ is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Highly selective mechanism-based thrombin inhibitors: structures of thrombin and trypsin inhibited with rigid peptidyl aldehydes., Krishnan R, Zhang E, Hakansson K, Arni RK, Tulinsky A, Lim-Wilby MS, Levy OE, Semple JE, Brunck TK, Biochemistry. 1998 Sep 1;37(35):12094-103. PMID:9724521

Page seeded by OCA on Sun Jul 27 19:54:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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