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.


1ijn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ijn.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ijn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ijn| PDB=1ijn | SCENE= }}
{{STRUCTURE_1ijn| PDB=1ijn | SCENE= }}
-
'''Crystal structure of the transthyretin mutant TTR C10A/Y114C'''
+
===Crystal structure of the transthyretin mutant TTR C10A/Y114C===
-
==Overview==
+
<!--
-
The Tyr114Cys substitution in the human plasma protein transthyretin leads to a particularly aggressive form of familial amyloidotic polyneuropathy. In a previous study we demonstrated that ATTR Tyr114Cys forms intermolecular disulfide bonds, which partly impair fibril formation and result in a more amorphous morphology. Apart from the introduced cysteinyl group in position 114, the native sequence contains one cysteine located at position 10. To deduce the role of intermolecular disulfide bridging in fibril formation we generated and characterized the TTR Cys10Ala/Tyr114Cys double mutant. Our results suggest that an intermolecular cysteine bridge at position 114 enhances the exposure of cysteine 10, thereby facilitating additional intermolecular cysteine assemblies. We also purified a disulfide-linked dimeric form of TTR Cys10Ala/Tyr114Cys, which was recognized by the anti-TTR amyloid-specific monoclonal antibody MAb (39-44). Moreover, this dimeric molecule can form protofibrils indistinguishable from the fibrils formed under reducing conditions, as judged by atomic force microscopy. Assuming that both molecules of the dimer are part of the core of the fibril, the assembly is incompatible with a preserved native or near-native dimeric interphase. Our findings raise the question of whether TTR-amyloid architecture is indeed the result of one highly stringent assembly of structures or if different fibrils may be built from different underlying structures.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16185074}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16185074 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16185074}}
==Disease==
==Disease==
Line 31: Line 35:
[[Category: Beta barrel]]
[[Category: Beta barrel]]
[[Category: Greek key]]
[[Category: Greek key]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:04:26 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 12:22:04 2008''

Revision as of 09:22, 1 July 2008

Image:1ijn.png

Template:STRUCTURE 1ijn

Contents

Crystal structure of the transthyretin mutant TTR C10A/Y114C

Template:ABSTRACT PUBMED 16185074

Disease

Known disease associated with this structure: Amyloid neuropathy, familial, several allelic types OMIM:[176300], Amyloidosis, senile systemic OMIM:[176300], Carpal tunnel syndrome, familial OMIM:[176300], Dystransthyretinemic hyperthyroxinemia OMIM:[176300]

About this Structure

1IJN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Cys114-linked dimers of transthyretin are compatible with amyloid formation., Karlsson A, Olofsson A, Eneqvist T, Sauer-Eriksson AE, Biochemistry. 2005 Oct 4;44(39):13063-70. PMID:16185074

Page seeded by OCA on Tue Jul 1 12:22:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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