1npo

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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1npo ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1npo ConSurf].
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== Publication Abstract from PubMed ==
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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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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<ref>PMID:8564543</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1npo" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
*[[Neurophysin|Neurophysin]]
*[[Neurophysin|Neurophysin]]
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 05:32, 5 June 2024

BOVINE NEUROPHYSIN II COMPLEX WITH OXYTOCIN

PDB ID 1npo

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