1npo

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(New page: 200px<br /><applet load="1npo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1npo, resolution 3.0&Aring;" /> '''BOVINE NEUROPHYSIN II...)
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[[Image:1npo.gif|left|200px]]<br /><applet load="1npo" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1npo, resolution 3.0&Aring;" />
caption="1npo, resolution 3.0&Aring;" />
'''BOVINE NEUROPHYSIN II COMPLEX WITH OXYTOCIN'''<br />
'''BOVINE NEUROPHYSIN II COMPLEX WITH OXYTOCIN'''<br />
==Overview==
==Overview==
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The first crystal structure of the pituitary hormone oxytocin complexed, with its carrier protein neurophysin has been determined and refined to, 3.0 A resolution. The hormone-binding site is located at the end of a, 3(10)-helix and involves residues from both domains of each monomer., Hormone residues Tyr 2, which is buried deep in the binding pocket, and, Cys 1 have been confirmed as the key residues involved in, neurophysin-hormone recognition. We have compared the bound oxytocin, observed in the neurophysin-oxytocin complex, the X-ray structures of, unbound oxytocin analogues and the NMR-derived structure for bound, oxytocin. We find that while our structure is in agreement with the, previous crystallographic findings, it differs from the NMR result with, regard to how Tyr 2 of the hormone is recognized by neurophysin.
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The first crystal structure of the pituitary hormone oxytocin complexed with its carrier protein neurophysin has been determined and refined to 3.0 A resolution. The hormone-binding site is located at the end of a 3(10)-helix and involves residues from both domains of each monomer. Hormone residues Tyr 2, which is buried deep in the binding pocket, and Cys 1 have been confirmed as the key residues involved in neurophysin-hormone recognition. We have compared the bound oxytocin observed in the neurophysin-oxytocin complex, the X-ray structures of unbound oxytocin analogues and the NMR-derived structure for bound oxytocin. We find that while our structure is in agreement with the previous crystallographic findings, it differs from the NMR result with regard to how Tyr 2 of the hormone is recognized by neurophysin.
==About this Structure==
==About this Structure==
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1NPO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NPO OCA].
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1NPO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPO OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Rose, J.P.]]
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[[Category: Rose, J P.]]
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[[Category: Wang, B.C.]]
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[[Category: Wang, B C.]]
[[Category: complex (hormone transport/hormone)]]
[[Category: complex (hormone transport/hormone)]]
[[Category: hypothalamus]]
[[Category: hypothalamus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:28:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:43 2008''

Revision as of 12:08, 21 February 2008


1npo, resolution 3.0Å

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BOVINE NEUROPHYSIN II COMPLEX WITH OXYTOCIN

Overview

The first crystal structure of the pituitary hormone oxytocin complexed with its carrier protein neurophysin has been determined and refined to 3.0 A resolution. The hormone-binding site is located at the end of a 3(10)-helix and involves residues from both domains of each monomer. Hormone residues Tyr 2, which is buried deep in the binding pocket, and Cys 1 have been confirmed as the key residues involved in neurophysin-hormone recognition. We have compared the bound oxytocin observed in the neurophysin-oxytocin complex, the X-ray structures of unbound oxytocin analogues and the NMR-derived structure for bound oxytocin. We find that while our structure is in agreement with the previous crystallographic findings, it differs from the NMR result with regard to how Tyr 2 of the hormone is recognized by neurophysin.

About this Structure

1NPO is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the neurophysin-oxytocin complex., Rose JP, Wu CK, Hsiao CD, Breslow E, Wang BC, Nat Struct Biol. 1996 Feb;3(2):163-9. PMID:8564543

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