2bn2: Difference between revisions

Revision as of 17:39, 21 February 2008

CRYSTAL STRUCTURE OF BOVINE NEUROPHYSIN II COMPLEXED WITH THE VASOPRESSIN ANALOGUE PHE-TYR AMIDE

OverviewOverview

The crystal structure of a dipeptide complex of bovine neurophysin II has been solved at 2.8 A resolution solely by using single-wavelength anomalous scattering data from a single iodinated derivative. The asymmetric unit is an elongated tetramer of dimensions 110 x 40 x 30 A, composed of two dimers related by pseudo twofold symmetry. Each monomer consists of two homologous layers, each with four antiparallel beta-strands. The two regions are connected by a helix followed by a long loop. Monomer-monomer contacts involve antiparallel beta-sheet interactions, which form a dimer with two layers of eight beta-strands. One peptide per monomer occupies the principal hormone-binding pocket formed by part of the amino-terminal region and parts of the connecting helix and loop, with binding to protein consistent with conclusions drawn from solution studies. Dimer-dimer contacts involve the Tyr49 region adjacent to this site. A fifth dipeptide, of unknown biological significance, helps to stabilize one of the monomer-monomer interfaces and the tetramer-tetramer network in the crystal.

About this StructureAbout this Structure

2BN2 is a Single protein structure of sequence from Bos taurus. This structure supersedes the now removed PDB entry 1BN2. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 A determined from the single-wavelength anomalous scattering signal of an incorporated iodine atom., Chen LQ, Rose JP, Breslow E, Yang D, Chang WR, Furey WF Jr, Sax M, Wang BC, Proc Natl Acad Sci U S A. 1991 May 15;88(10):4240-4. PMID:2034668

Page seeded by OCA on Thu Feb 21 16:39:31 2008

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

OCA

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-[[Image:2bn2.gif|left|200px]]<br /><applet load="2bn2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2bn2.gif|left|200px]]<br /><applet load="2bn2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2bn2, resolution 2.80&Aring;" />
 '''CRYSTAL STRUCTURE OF BOVINE NEUROPHYSIN II COMPLEXED WITH THE VASOPRESSIN ANALOGUE PHE-TYR AMIDE'''<br />
 ==Overview==
-The crystal structure of a dipeptide complex of bovine neurophysin II has, been solved at 2.8 A resolution solely by using single-wavelength, anomalous scattering data from a single iodinated derivative. The, asymmetric unit is an elongated tetramer of dimensions 110 x 40 x 30 A, composed of two dimers related by pseudo twofold symmetry. Each monomer, consists of two homologous layers, each with four antiparallel, beta-strands. The two regions are connected by a helix followed by a long, loop. Monomer-monomer contacts involve antiparallel beta-sheet, interactions, which form a dimer with two layers of eight beta-strands., One peptide per monomer occupies the principal hormone-binding pocket, formed by part of the amino-terminal region and parts of the connecting, helix and loop, with binding to protein consistent with conclusions drawn, from solution studies. Dimer-dimer contacts involve the Tyr49 region, adjacent to this site. A fifth dipeptide, of unknown biological, significance, helps to stabilize one of the monomer-monomer interfaces and, the tetramer-tetramer network in the crystal.
+The crystal structure of a dipeptide complex of bovine neurophysin II has been solved at 2.8 A resolution solely by using single-wavelength anomalous scattering data from a single iodinated derivative. The asymmetric unit is an elongated tetramer of dimensions 110 x 40 x 30 A, composed of two dimers related by pseudo twofold symmetry. Each monomer consists of two homologous layers, each with four antiparallel beta-strands. The two regions are connected by a helix followed by a long loop. Monomer-monomer contacts involve antiparallel beta-sheet interactions, which form a dimer with two layers of eight beta-strands. One peptide per monomer occupies the principal hormone-binding pocket formed by part of the amino-terminal region and parts of the connecting helix and loop, with binding to protein consistent with conclusions drawn from solution studies. Dimer-dimer contacts involve the Tyr49 region adjacent to this site. A fifth dipeptide, of unknown biological significance, helps to stabilize one of the monomer-monomer interfaces and the tetramer-tetramer network in the crystal.
 ==About this Structure==
-BN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure superseeds the now removed PDB entry 1BN2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BN2 OCA].
+BN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry 1BN2. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BN2 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Bos taurus]]
 [[Category: Single protein]]
-[[Category: Rose, J.P.]]
+[[Category: Rose, J P.]]
-[[Category: Wang, B.C.]]
+[[Category: Wang, B C.]]
 [[Category: complex (protein/hormone)]]
 [[Category: hormone packaging]]
 [[Category: transport]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:50:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:39:31 2008''