1qu1: Difference between revisions

Revision as of 15:43, 21 February 2008

CRYSTAL STRUCTURE OF EHA2 (23-185)

OverviewOverview

The structure of a stable recombinant ectodomain of influenza hemagglutinin HA(2) subunit, EHA(2) (23-185), defined by proteolysis studies of the intact bacterial-expressed ectodomain, was determined to 1.9-A resolution by using x-ray crystallography. The structure reveals a domain composed of N- and C-terminal residues that form an N cap terminating both the N-terminal alpha-helix and the central coiled coil. The N cap is formed by a conserved sequence, and part of it is found in the neutral pH conformation of HA. The C-terminal 23 residues of the ectodomain form a 72-A long nonhelical structure ordered to within 7 residues of the transmembrane anchor. The structure implies that continuous alpha helices are not required for membrane fusion at either the N or C termini. The difference in stability between recombinant molecules with and without the N cap sequences suggests that additional free energy for membrane fusion may become available after the formation of the central triple-stranded coiled coil and insertion of the fusion peptide into the target membrane.

About this StructureAbout this Structure

1QU1 is a Single protein structure of sequence from Influenza a virus. The following page contains interesting information on the relation of 1QU1 with [Hemagglutinin]. Full crystallographic information is available from OCA.

ReferenceReference

N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil., Chen J, Skehel JJ, Wiley DC, Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8967-72. PMID:10430879

Page seeded by OCA on Thu Feb 21 14:43:40 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1qu1.gif|left|200px]]<br />
+[[Image:1qu1.gif|left|200px]]<br /><applet load="1qu1" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1qu1" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1qu1, resolution 1.90&Aring;" />
 '''CRYSTAL STRUCTURE OF EHA2 (23-185)'''<br />
 ==Overview==
-The structure of a stable recombinant ectodomain of influenza, hemagglutinin HA(2) subunit, EHA(2) (23-185), defined by proteolysis, studies of the intact bacterial-expressed ectodomain, was determined to, 1.9-A resolution by using x-ray crystallography. The structure reveals a, domain composed of N- and C-terminal residues that form an N cap, terminating both the N-terminal alpha-helix and the central coiled coil., The N cap is formed by a conserved sequence, and part of it is found in, the neutral pH conformation of HA. The C-terminal 23 residues of the, ectodomain form a 72-A long nonhelical structure ordered to within 7, residues of the transmembrane anchor. The structure implies that, continuous alpha helices are not required for membrane fusion at either, the N or C termini. The difference in stability between recombinant, molecules with and without the N cap sequences suggests that additional, free energy for membrane fusion may become available after the formation, of the central triple-stranded coiled coil and insertion of the fusion, peptide into the target membrane.
+The structure of a stable recombinant ectodomain of influenza hemagglutinin HA(2) subunit, EHA(2) (23-185), defined by proteolysis studies of the intact bacterial-expressed ectodomain, was determined to 1.9-A resolution by using x-ray crystallography. The structure reveals a domain composed of N- and C-terminal residues that form an N cap terminating both the N-terminal alpha-helix and the central coiled coil. The N cap is formed by a conserved sequence, and part of it is found in the neutral pH conformation of HA. The C-terminal 23 residues of the ectodomain form a 72-A long nonhelical structure ordered to within 7 residues of the transmembrane anchor. The structure implies that continuous alpha helices are not required for membrane fusion at either the N or C termini. The difference in stability between recombinant molecules with and without the N cap sequences suggests that additional free energy for membrane fusion may become available after the formation of the central triple-stranded coiled coil and insertion of the fusion peptide into the target membrane.
 ==About this Structure==
-QU1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. The following page contains interesting information on the relation of 1QU1 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb76_1.html Hemagglutinin]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QU1 OCA].
+QU1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. The following page contains interesting information on the relation of 1QU1 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb76_1.html Hemagglutinin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QU1 OCA].
 ==Reference==
@@ Line 16: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Chen, J.]]
-[[Category: Skehel, J.J.]]
+[[Category: Skehel, J J.]]
-[[Category: Wiley, D.C.]]
+[[Category: Wiley, D C.]]
 [[Category: hemagglutinin]]
 [[Category: low-ph]]
 [[Category: virus/viral protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:05:12 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:40 2008''