2oct

From Proteopedia

Revision as of 21:02, 12 November 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search
Image:2oct.gif

2oct, resolution 1.4Å

Drag the structure with the mouse to rotate

Stefin B (Cystatin B) tetramer

Contents

Overview

Here we present the tetrameric structure of stefin B, which is the result, of a process by which two domain-swapped dimers of stefin B are, transformed into tetramers. The transformation involves a previously, unidentified process of extensive intermolecular contacts, termed hand, shaking, which occurs concurrently with trans to cis isomerization of, proline 74. This proline residue is widely conserved throughout the, cystatin superfamily, a member of which, human cystatin C, is the key, protein in cerebral amyloid angiopathy. These results are consistent with, the hypothesis that isomerization of proline residues can play a decisive, role in amyloidogenesis.

Disease

Known diseases associated with this structure: Epilepsy, progressive myoclonic 1 OMIM:[601145]

About this Structure

2OCT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Essential role of proline isomerization in stefin B tetramer formation., Jenko Kokalj S, Guncar G, Stern I, Morgan G, Rabzelj S, Kenig M, Staniforth RA, Waltho JP, Zerovnik E, Turk D, J Mol Biol. 2007 Mar 9;366(5):1569-79. Epub 2006 Dec 16. PMID:17217964

Page seeded by OCA on Mon Nov 12 23:09:22 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

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