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.


2ggz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ggz.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2ggz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ggz| PDB=2ggz | SCENE= }}
{{STRUCTURE_2ggz| PDB=2ggz | SCENE= }}
-
'''Crystal Structure of Human Guanylate Cyclase Activating Protein-3'''
+
===Crystal Structure of Human Guanylate Cyclase Activating Protein-3===
-
==Overview==
+
<!--
-
Absorption of light by visual pigments initiates the phototransduction pathway that results in degradation of the intracellular pool of cyclic-GMP (cGMP). This hydrolysis promotes the closing of cGMP-gated cation channels and consequent hyperpolarization of rod and cone photoreceptor cell membranes. Guanylate cyclase-activating proteins (GCAPs) are a family of proteins that regulate retinal guanylate cyclase (GC) activity in a Ca2+-dependent manner. At high [Ca2+], typical of the dark-adapted state (approximately 500 nM), GCAPs inhibit retinal GCs. At the low [Ca2+] (approximately 50 nM) that occurs after the closing of cGMP-gated channels, GCAPs activate retinal GCs to replenish dark-state cGMP levels. Here, we report the crystal structure of unmyristoylated human GCAP3 with Ca2+ bound. GCAP3 is an EF-hand Ca2+-binding protein with Ca2+ bound to EF2, 3 and 4, while Ca2+ binding to EF-hand 1 is disabled. GCAP3 contains two domains with the EF-hand motifs arranged in a tandem array similar to GCAP2 and members of the recoverin subfamily of Ca2+-binding proteins. Residues not involved in Ca2+ binding, but conserved in all GCAPs, cluster around EF1 in the N-terminal domain and may represent the interface with GCs. Five point mutations in the closely related GCAP1 have been linked to the etiology of cone dystrophies. These residues are conserved in GCAP3 and the structure suggests important roles for these amino acids. We present a homology model of GCAP1 based on GCAP3 that offers insight into the molecular mechanism underlying the autosomal dominant cone dystrophies produced by GCAP1 mutations.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16626734}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16626734 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16626734}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Gcap3]]
[[Category: Gcap3]]
[[Category: Guanylate cyclase activating protein]]
[[Category: Guanylate cyclase activating protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:05:46 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:04:49 2008''

Revision as of 13:04, 29 July 2008

Image:2ggz.png

Template:STRUCTURE 2ggz

Crystal Structure of Human Guanylate Cyclase Activating Protein-3

Template:ABSTRACT PUBMED 16626734

About this Structure

2GGZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of GCAP3 suggests molecular mechanism of GCAP-linked cone dystrophies., Stephen R, Palczewski K, Sousa MC, J Mol Biol. 2006 Jun 2;359(2):266-75. Epub 2006 Apr 3. PMID:16626734

Page seeded by OCA on Tue Jul 29 16:04:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ggz"
Personal tools