2acp: Difference between revisions

Revision as of 16:49, 22 September 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:2acp.png

Template:STRUCTURE 2acp

Crystal structure of nitrophorin 2 aqua complexCrystal structure of nitrophorin 2 aqua complex

Template:ABSTRACT PUBMED 10884386

About this StructureAbout this Structure

2ACP is a Single protein structure of sequence from Rhodnius prolixus. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of nitrophorin 2. A trifunctional antihemostatic protein from the saliva of Rhodnius prolixus., Andersen JF, Montfort WR, J Biol Chem. 2000 Sep 29;275(39):30496-503. PMID:10884386

Page seeded by OCA on Mon Sep 22 16:49:35 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2acp.gif|left|200px]]
+{{Seed}}
+[[Image:2acp.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2acp|  PDB=2acp  |  SCENE=  }}
-'''Crystal structure of nitrophorin 2 aqua complex'''
+===Crystal structure of nitrophorin 2 aqua complex===
-==Overview==
+<!--
-Nitrophorin 2 (NP2) (also known as prolixin-S) is a salivary protein that transports nitric oxide, binds histamine, and acts as an anticoagulant during blood feeding by the insect Rhodnius prolixus. The 2.0-A crystal structure of NP2 reveals an eight-stranded antiparallel beta-barrel containing a ferric heme coordinated through His(57), similar to the structures of NP1 and NP4. All four Rhodnius nitrophorins transport NO and sequester histamine through heme binding, but only NP2 acts as an anticoagulant. Here, we demonstrate that recombinant NP2, but not recombinant NP1 or NP4, is a potent anticoagulant; recombinant NP3 also displays minor activity. Comparison of the nitrophorin structures suggests that a surface region near the C terminus and the loops between beta strands B-C and E-F is responsible for the anticoagulant activity. NP2 also displays larger NO association rates and smaller dissociation rates than NP1 and NP4, which may result from a more open and more hydrophobic distal pocket, allowing more rapid solvent reorganization on ligand binding. The NP2 protein core differs from NP1 and NP4 in that buried Glu(53), which allows for larger NO release rates when deprotonated, hydrogen bonds to invariant Tyr(81). Surprisingly, this tyrosine lies on the protein surface in NP1 and NP4.
+The line below this paragraph, {{ABSTRACT_PUBMED_10884386}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10884386 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10884386}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Ferrous heme]]
 [[Category: Lipocalin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:53:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Sep 22 16:49:35 2008''