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.


1tul

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1tul.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1tul.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1tul| PDB=1tul | SCENE= }}
{{STRUCTURE_1tul| PDB=1tul | SCENE= }}
-
'''STRUCTURE OF TLP20'''
+
===STRUCTURE OF TLP20===
-
==Overview==
+
<!--
-
Myosin light-chain kinase is responsible for the phosphorylation of myosin in smooth muscle cells. In some tissue types, the C-terminal portion of this large enzyme is expressed as an independent protein and has been given the name telokin. Recently, an antibody directed against telokin was found to interact with a protein derived from the baculovirus Autographa californica nuclear polyhedrosis virus. This protein was biochemically characterized and given the name TLP20 for telokin-like protein of 20 000 molecular weight. The amino-acid sequence of TLP20 was determined on the basis of a cDNA clone and subsequent alignment searches failed to reveal any homology to telokin or to other known proteins. The three-dimensional structure of a proteolytic portion of TLP20 is reported here. Crystals employed in the investigation were grown from ammonium sulfate solutions at pH 6.0 and belonged to the space group P2(1)3 with unit-cell dimensions of a = b = c = 76.3 A and one molecule per asymmetric unit. The structure was determined by multiple isomorphous replacement with three heavy-atom derivatives. Least-squares refinement of the model reduced the crystallographic R factor to 18.1% for all measured X-ray data from 30.0 to 2.2 A. The overall fold of the molecule may be described as a seven-stranded antiparallel beta-barrel flanked on the bottom by two additional beta-strands and on the top by an alpha-helix. Quite surprisingly, the three-dimensional structure of this beta-barrel is not similar to telokin or to any other known protein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15299576}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15299576 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15299576}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Rayment, I.]]
[[Category: Rayment, I.]]
[[Category: Telokin-like protein]]
[[Category: Telokin-like protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:23:09 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:22:26 2008''

Revision as of 11:22, 27 July 2008

Image:1tul.png

Template:STRUCTURE 1tul

STRUCTURE OF TLP20

Template:ABSTRACT PUBMED 15299576

About this Structure

1TUL is a Single protein structure of sequence from Autographa californica nucleopolyhedrovirus. Full crystallographic information is available from OCA.

Reference

Molecular structure of a proteolytic fragment of TLP20., Holden HM, Wesenberg G, Raynes DA, Hartshorne DJ, Guerriero V Jr, Rayment I, Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1153-60. PMID:15299576

Page seeded by OCA on Sun Jul 27 14:22:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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