2oct

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Revision as of 21:02, 12 November 2007

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spinqualitylabelsall models 2oct, resolution 1.4Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Stefin B (Cystatin B) tetramer

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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

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