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.

2gbf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2gbf.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2gbf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2gbf| PDB=2gbf | SCENE= }}
{{STRUCTURE_2gbf| PDB=2gbf | SCENE= }}
-
'''rat dpp-IV with alkynyl cyanopyrrolidine #1'''
+
===rat dpp-IV with alkynyl cyanopyrrolidine #1===
-
==Overview==
+
<!--
-
Dipeptidyl peptidase IV (DPP-IV) belongs to a family of serine peptidases, and due to its indirect regulatory role in plasma glucose modulation, DPP-IV has become an attractive pharmaceutical target for diabetes therapy. DPP-IV inactivates the glucagon-like peptide (GLP-1) and several other naturally produced bioactive peptides that contain preferentially a proline or alanine residue in the second amino acid sequence position by cleaving the N-terminal dipeptide. To elucidate the details of the active site for structure-based drug design, we crystallized a natural source preparation of DPP-IV isolated from rat kidney and determined its three-dimensional structure using X-ray diffraction techniques. With a high degree of similarity to structures of human DPP-IV, the active site architecture provides important details for the design of inhibitory compounds, and structures of inhibitor-protein complexes offer detailed insight into three-dimensional structure-activity relationships that include a conformational change of Tyr548. Such accommodation is exemplified by the response to chemical substitution on 2-cyanopyrrolidine inhibitors at the 5 position, which conveys inhibitory selectivity for DPP-IV over closely related homologues. A similar conformational change is also observed in the complex with an unrelated synthetic inhibitor containing a xanthine core that is also selective for DPP-IV. These results suggest the conformational flexibility of Tyr548 is unique among protein family members and may be utilized in drug design to achieve peptidase selectivity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16768443}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16768443 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16768443}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Wilk, S.]]
[[Category: Wilk, S.]]
[[Category: Serine peptidase beta propeller]]
[[Category: Serine peptidase beta propeller]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:54:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:45:45 2008''

Revision as of 12:45, 28 July 2008

Image:2gbf.png

Template:STRUCTURE 2gbf

rat dpp-IV with alkynyl cyanopyrrolidine #1

Template:ABSTRACT PUBMED 16768443

About this Structure

2GBF is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structures of DPP-IV (CD26) from rat kidney exhibit flexible accommodation of peptidase-selective inhibitors., Longenecker KL, Stewart KD, Madar DJ, Jakob CG, Fry EH, Wilk S, Lin CW, Ballaron SJ, Stashko MA, Lubben TH, Yong H, Pireh D, Pei Z, Basha F, Wiedeman PE, von Geldern TW, Trevillyan JM, Stoll VS, Biochemistry. 2006 Jun 20;45(24):7474-82. PMID:16768443

Page seeded by OCA on Mon Jul 28 15:45:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2gbf"
Personal tools