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.


1ryp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ryp.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ryp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ryp| PDB=1ryp | SCENE= }}
{{STRUCTURE_1ryp| PDB=1ryp | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE 20S PROTEASOME FROM YEAST AT 2.4 ANGSTROMS RESOLUTION'''
+
===CRYSTAL STRUCTURE OF THE 20S PROTEASOME FROM YEAST AT 2.4 ANGSTROMS RESOLUTION===
-
==Overview==
+
<!--
-
The crystal structure of the 20S proteasome from the yeast Saccharomyces cerevisiae shows that its 28 protein subunits are arranged as an (alpha1...alpha7, beta1...beta7)2 complex in four stacked rings and occupy unique locations. The interior of the particle, which harbours the active sites, is only accessible by some very narrow side entrances. The beta-type subunits are synthesized as proproteins before being proteolytically processed for assembly into the particle. The proforms of three of the seven different beta-type subunits, beta1/PRE3, beta2/PUP1 and beta5/PRE2, are cleaved between the threonine at position 1 and the last glycine of the pro-sequence, with release of the active-site residue Thr 1. These three beta-type subunits have inhibitor-binding sites, indicating that PRE2 has a chymotrypsin-like and a trypsin-like activity and that PRE3 has peptidylglutamyl peptide hydrolytic specificity. Other beta-type subunits are processed to an intermediate form, indicating that an additional nonspecific endopeptidase activity may exist which is important for peptide hydrolysis and for the generation of ligands for class I molecules of the major histocompatibility complex.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9087403}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9087403 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9087403}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Protease]]
[[Category: Protease]]
[[Category: Protein degradation]]
[[Category: Protein degradation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:04:25 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:02:41 2008''

Revision as of 18:02, 28 July 2008

Image:1ryp.png

Template:STRUCTURE 1ryp

CRYSTAL STRUCTURE OF THE 20S PROTEASOME FROM YEAST AT 2.4 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 9087403

About this Structure

1RYP is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structure of 20S proteasome from yeast at 2.4 A resolution., Groll M, Ditzel L, Lowe J, Stock D, Bochtler M, Bartunik HD, Huber R, Nature. 1997 Apr 3;386(6624):463-71. PMID:9087403

Page seeded by OCA on Mon Jul 28 21:02:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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