Essential role of proline isomerization in stefin B tetramer formation.

Sasa Jenko Kokalj; Gregor Guncar; Igor Stern; Gareth Morgan; Sabina Rabzelj; Manca Kenig; Rosemary A Staniforth; Jonathan P Waltho; Eva Zerovnik; Dusan Turk; Saša Jenko Kokalj; Gregor Gunčar; Eva Žerovnik; Dušan Turk

doi:10.1016/j.jmb.2006.12.025

Essential role of proline isomerization in stefin B tetramer formation.

Sasa Jenko Kokalj, Gregor Guncar, Igor Stern, Gareth Morgan, Sabina Rabzelj, Manca Kenig, Rosemary A Staniforth, Jonathan P Waltho, Eva Zerovnik, Dusan Turk, Saša Jenko Kokalj, Gregor Gunčar, Eva Žerovnik, Dušan Turk

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	1569-1579
Number of pages	10
Journal	Journal of molecular biology
Volume	366
Issue number	5
DOIs	https://doi.org/10.1016/j.jmb.2006.12.025
Publication status	Published - 9 Mar 2007

Keywords

amyloid
crystal structure
cystatin
domain-swapping
stefin

Access to Document

10.1016/j.jmb.2006.12.025

Cite this

@article{87dc570fd0cd45bdae26d29e7ddfc4a8,

title = "Essential role of proline isomerization in stefin B tetramer formation.",

abstract = "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.",

keywords = "amyloid, crystal structure, cystatin, domain-swapping, stefin",

author = "{Jenko Kokalj}, Sasa and Gregor Guncar and Igor Stern and Gareth Morgan and Sabina Rabzelj and Manca Kenig and Staniforth, {Rosemary A} and Waltho, {Jonathan P} and Eva Zerovnik and Dusan Turk and {Jenko Kokalj}, Sa{\v s}a and Gregor Gun{\v c}ar and Eva {\v Z}erovnik and Du{\v s}an Turk",

year = "2007",

month = mar,

day = "9",

doi = "10.1016/j.jmb.2006.12.025",

language = "English",

volume = "366",

pages = "1569--1579",

journal = "Journal of molecular biology",

issn = "1089-8638",

publisher = "Academic Press, Ltd",

number = "5",

}

TY - JOUR

T1 - Essential role of proline isomerization in stefin B tetramer formation.

AU - Jenko Kokalj, Sasa

AU - Guncar, Gregor

AU - Stern, Igor

AU - Morgan, Gareth

AU - Rabzelj, Sabina

AU - Kenig, Manca

AU - Staniforth, Rosemary A

AU - Waltho, Jonathan P

AU - Zerovnik, Eva

AU - Turk, Dusan

AU - Jenko Kokalj, Saša

AU - Gunčar, Gregor

AU - Žerovnik, Eva

AU - Turk, Dušan

PY - 2007/3/9

Y1 - 2007/3/9

N2 - 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.

AB - 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.

KW - amyloid

KW - crystal structure

KW - cystatin

KW - domain-swapping

KW - stefin

U2 - 10.1016/j.jmb.2006.12.025

DO - 10.1016/j.jmb.2006.12.025

M3 - Article

C2 - 17217964

SN - 1089-8638

VL - 366

SP - 1569

EP - 1579

JO - Journal of molecular biology

JF - Journal of molecular biology

IS - 5

ER -

Essential role of proline isomerization in stefin B tetramer formation.

Abstract

Keywords

Access to Document

Fingerprint

Cite this