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.


1ucp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ucp.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ucp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ucp| PDB=1ucp | SCENE= }}
{{STRUCTURE_1ucp| PDB=1ucp | SCENE= }}
-
'''NMR structure of the PYRIN domain of human ASC'''
+
===NMR structure of the PYRIN domain of human ASC===
-
==Overview==
+
<!--
-
The PYRIN domain is a conserved sequence motif identified in more than 20 human proteins with putative functions in apoptotic and inflammatory signalling pathways. The three-dimensional structure of the PYRIN domain from human ASC was determined by NMR spectroscopy. The structure determination reveals close structural similarity to death domains, death effector domains, and caspase activation and recruitment domains, although the structural alignment with these other members of the death-domain superfamily differs from previously predicted amino acid sequence alignments. Two highly positively and negatively charged surfaces in the PYRIN domain of ASC result in a strong electrostatic dipole moment that is predicted to be present also in related PYRIN domains. These results suggest that electrostatic interactions play an important role for the binding between PYRIN domains. Consequently, the previously reported binding between the PYRIN domains of ASC and ASC2/POP1 or between the zebrafish PYRIN domains of zAsc and Caspy is proposed to involve interactions between helices 2 and 3 of one PYRIN domain with helices 1 and 4 of the other PYRIN domain, in analogy to previously reported homophilic interactions between caspase activation and recruitment domains.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14499617}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14499617 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14499617}}
==About this Structure==
==About this Structure==
-
1UCP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UCP OCA].
+
1UCP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UCP OCA].
==Reference==
==Reference==
Line 29: Line 33:
[[Category: Staub, E.]]
[[Category: Staub, E.]]
[[Category: Death domain fold]]
[[Category: Death domain fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:02:46 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:22:45 2008''

Revision as of 13:22, 27 July 2008

Image:1ucp.png

Template:STRUCTURE 1ucp

NMR structure of the PYRIN domain of human ASC

Template:ABSTRACT PUBMED 14499617

About this Structure

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

Reference

The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition., Liepinsh E, Barbals R, Dahl E, Sharipo A, Staub E, Otting G, J Mol Biol. 2003 Oct 3;332(5):1155-63. PMID:14499617

Page seeded by OCA on Sun Jul 27 16:22:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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