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.


1vhh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vhh.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1vhh.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vhh| PDB=1vhh | SCENE= }}
{{STRUCTURE_1vhh| PDB=1vhh | SCENE= }}
-
'''A POTENTIAL CATALYTIC SITE WITHIN THE AMINO-TERMINAL SIGNALLING DOMAIN OF SONIC HEDGEHOG'''
+
===A POTENTIAL CATALYTIC SITE WITHIN THE AMINO-TERMINAL SIGNALLING DOMAIN OF SONIC HEDGEHOG===
-
==Overview==
+
<!--
-
Within the past few years, members of the hedgehog (hh) family of secreted signalling proteins have emerged as the primary signals generated by certain embryonic patterning centres. In vertebrate embryos, for example, sonic hedgehog expression in the notochord appears to be responsible for the local and long-range induction of ventral cell types within the neural tube and somites (reviewed in refs 1, 2). Protein products encoded by hh family members are synthesized as precursors that undergo autoprocessing to generate an amino-terminal domain that appears to be responsible for both local and long-range signalling activities, and a carboxy-terminal domain that contains the autoprocessing activity. As part of an effort to understand how hh family members participate in cell-to-cell signalling, we have determined and report here the crystal structure at 1.7 A of the amino-terminal domain of murine Sonic hedgehog (Shh-N). The structure revealed a tetrahedrally coordinated zinc ion that appears to be structurally analogous to the zinc coordination sites of zinc hydrolases, such as thermolysin and carboxypeptidase A. This previously unsuspected catalytic site represents a distinct activity from the autoprocessing activity that resides in the carboxy-terminal domain.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7477329}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7477329 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7477329}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Porter, J A.]]
[[Category: Porter, J A.]]
[[Category: Signalling protein]]
[[Category: Signalling protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:32:33 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:53:28 2008''

Revision as of 09:53, 28 July 2008

Image:1vhh.png

Template:STRUCTURE 1vhh

A POTENTIAL CATALYTIC SITE WITHIN THE AMINO-TERMINAL SIGNALLING DOMAIN OF SONIC HEDGEHOG

Template:ABSTRACT PUBMED 7477329

About this Structure

1VHH is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

A potential catalytic site revealed by the 1.7-A crystal structure of the amino-terminal signalling domain of Sonic hedgehog., Hall TM, Porter JA, Beachy PA, Leahy DJ, Nature. 1995 Nov 9;378(6553):212-6. PMID:7477329

Page seeded by OCA on Mon Jul 28 12:53:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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