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.

1pso

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1pso.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1pso.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1pso| PDB=1pso | SCENE= }}
{{STRUCTURE_1pso| PDB=1pso | SCENE= }}
-
'''THE CRYSTAL STRUCTURE OF HUMAN PEPSIN AND ITS COMPLEX WITH PEPSTATIN'''
+
===THE CRYSTAL STRUCTURE OF HUMAN PEPSIN AND ITS COMPLEX WITH PEPSTATIN===
-
==Overview==
+
<!--
-
The three-dimensional crystal structure of human pepsin and that of its complex with pepstatin have been solved by X-ray crystallographic methods. The native pepsin structure has been refined with data collected to 2.2 A resolution to an R-factor of 19.7%. The pepsin:pepstatin structure has been refined with data to 2.0 A resolution to an R-factor of 18.5%. The hydrogen bonding interactions and the conformation adopted by pepstatin are very similar to those found in complexes of pepstatin with other aspartic proteinases. The enzyme undergoes a conformational change upon inhibitor binding to enclose the inhibitor more tightly. The analysis of the binding sites indicates that they form an extended tube without distinct binding pockets. By comparing the residues on the binding surface with those of the other human aspartic proteinases, it has been possible to rationalize some of the experimental data concerning the different specificities. At the S1 site, valine at position 120 in renin instead of isoleucine, as in the other enzymes, allows for binding of larger hydrophobic residues. The possibility of multiple conformations for the P2 residue makes the analysis of the S2 site difficult. However, it is possible to see that the specific interactions that renin makes with histidine at P2 would not be possible in the case of the other enzymes. At the S3 site, the smaller volume that is accessible in pepsin compared to the other enzymes is consistent with its preference for smaller residues at the P3 position.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7663352}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7663352 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7663352}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Mosimann, S C.]]
[[Category: Mosimann, S C.]]
[[Category: Tarasova, N.]]
[[Category: Tarasova, N.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:26:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:49:35 2008''

Revision as of 08:49, 28 July 2008

Image:1pso.png

Template:STRUCTURE 1pso

THE CRYSTAL STRUCTURE OF HUMAN PEPSIN AND ITS COMPLEX WITH PEPSTATIN

Template:ABSTRACT PUBMED 7663352

About this Structure

1PSO is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Crystal structure of human pepsin and its complex with pepstatin., Fujinaga M, Chernaia MM, Tarasova NI, Mosimann SC, James MN, Protein Sci. 1995 May;4(5):960-72. PMID:7663352

Page seeded by OCA on Mon Jul 28 11:49:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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