1tb5: Difference between revisions

Revision as of 21:41, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1tb5.png

Template:STRUCTURE 1tb5

Catalytic Domain Of Human Phosphodiesterase 4B In Complex With AMPCatalytic Domain Of Human Phosphodiesterase 4B In Complex With AMP

Template:ABSTRACT PUBMED 15260978

About this StructureAbout this Structure

1TB5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases., Zhang KY, Card GL, Suzuki Y, Artis DR, Fong D, Gillette S, Hsieh D, Neiman J, West BL, Zhang C, Milburn MV, Kim SH, Schlessinger J, Bollag G, Mol Cell. 2004 Jul 23;15(2):279-86. PMID:15260978

Page seeded by OCA on Mon Jul 28 21:41:49 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1tb5.gif|left|200px]]
+{{Seed}}
+[[Image:1tb5.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1tb5|  PDB=1tb5  |  SCENE=  }}
-'''Catalytic Domain Of Human Phosphodiesterase 4B In Complex With AMP'''
+===Catalytic Domain Of Human Phosphodiesterase 4B In Complex With AMP===
-==Overview==
+<!--
-Phosphodiesterases (PDEs) comprise a family of enzymes that modulate the immune response, inflammation, and memory, among many other functions. There are three types of PDEs: cAMP-specific, cGMP-specific, and dual-specific. Here we describe the mechanism of nucleotide selectivity on the basis of high-resolution co-crystal structures of the cAMP-specific PDE4B and PDE4D with AMP, the cGMP-specific PDE5A with GMP, and the apo-structure of the dual-specific PDE1B. These structures show that an invariant glutamine functions as the key specificity determinant by a "glutamine switch" mechanism for recognizing the purine moiety in cAMP or cGMP. The surrounding residues anchor the glutamine residue in different orientations for cAMP and for cGMP. The PDE1B structure shows that in dual-specific PDEs a key histidine residue may enable the invariant glutamine to toggle between cAMP and cGMP. The structural understanding of nucleotide binding enables the design of new PDE inhibitors that may treat diseases in which cyclic nucleotides play a critical role.
+The line below this paragraph, {{ABSTRACT_PUBMED_15260978}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15260978 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15260978}}
 ==About this Structure==
@@ Line 38: / Line 42: @@
 [[Category: Zhang, K Y.J.]]
 [[Category: Pde4b]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:45:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:41:49 2008''