1jk4: Difference between revisions
New page: left|200px<br /><applet load="1jk4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jk4, resolution 2.3Å" /> '''DES 1-6 BOVINE NEUROP... |
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[[Image:1jk4.gif|left|200px]]<br /><applet load="1jk4" size=" | [[Image:1jk4.gif|left|200px]]<br /><applet load="1jk4" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1jk4, resolution 2.3Å" /> | caption="1jk4, resolution 2.3Å" /> | ||
'''DES 1-6 BOVINE NEUROPHYSIN II COMPLEX WITH VASOPRESSIN'''<br /> | '''DES 1-6 BOVINE NEUROPHYSIN II COMPLEX WITH VASOPRESSIN'''<br /> | ||
==Overview== | ==Overview== | ||
The structures of des 1-6 bovine neurophysin-II in the unliganded state | The structures of des 1-6 bovine neurophysin-II in the unliganded state and as its complex with lysine vasopressin were determined crystallographically at resolutions of 2.4 A and 2.3 A, respectively. The structure of the protein component of the vasopressin complex was, with some local differences, similar to that determined earlier of the full-length protein complexed with oxytocin, but relatively large differences, probably intrinsic to the hormones, were observed between the structures of bound oxytocin and bound vasopressin at Gln 4. The structure of the unliganded protein is the first structure of an unliganded neurophysin. Comparison with the liganded state indicated significant binding-induced conformational changes that were the largest in the loop region comprising residues 50-58 and in the 7-10 region. A subtle binding-induced tightening of the subunit interface of the dimer also was shown, consistent with a role for interface changes in neurophysin allosteric mechanism, but one that is probably not predominant. Interface changes are suggested to be communicated from the binding site through the strands of beta-sheet that connect these two regions, in part with mediation by Gly 23. Comparison of unliganded and liganded states additionally reveals that the binding site for the hormone alpha-amino group is largely preformed and accessible in the unliganded state, suggesting that it represents the initial site of hormone protein recognition. The potential molecular basis for its thermodynamic contribution to binding is discussed. | ||
==About this Structure== | ==About this Structure== | ||
1JK4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1JK4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JK4 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rose, J | [[Category: Rose, J P.]] | ||
[[Category: Wang, B | [[Category: Wang, B C.]] | ||
[[Category: CD]] | [[Category: CD]] | ||
[[Category: complex (hormone transport/hormone)]] | [[Category: complex (hormone transport/hormone)]] | ||
[[Category: hypothalamus]] | [[Category: hypothalamus]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:34 2008'' | ||
Revision as of 14:23, 21 February 2008
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DES 1-6 BOVINE NEUROPHYSIN II COMPLEX WITH VASOPRESSIN
OverviewOverview
The structures of des 1-6 bovine neurophysin-II in the unliganded state and as its complex with lysine vasopressin were determined crystallographically at resolutions of 2.4 A and 2.3 A, respectively. The structure of the protein component of the vasopressin complex was, with some local differences, similar to that determined earlier of the full-length protein complexed with oxytocin, but relatively large differences, probably intrinsic to the hormones, were observed between the structures of bound oxytocin and bound vasopressin at Gln 4. The structure of the unliganded protein is the first structure of an unliganded neurophysin. Comparison with the liganded state indicated significant binding-induced conformational changes that were the largest in the loop region comprising residues 50-58 and in the 7-10 region. A subtle binding-induced tightening of the subunit interface of the dimer also was shown, consistent with a role for interface changes in neurophysin allosteric mechanism, but one that is probably not predominant. Interface changes are suggested to be communicated from the binding site through the strands of beta-sheet that connect these two regions, in part with mediation by Gly 23. Comparison of unliganded and liganded states additionally reveals that the binding site for the hormone alpha-amino group is largely preformed and accessible in the unliganded state, suggesting that it represents the initial site of hormone protein recognition. The potential molecular basis for its thermodynamic contribution to binding is discussed.
About this StructureAbout this Structure
1JK4 is a Protein complex structure of sequences from Bos taurus with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structures of an unliganded neurophysin and its vasopressin complex: implications for binding and allosteric mechanisms., Wu CK, Hu B, Rose JP, Liu ZJ, Nguyen TL, Zheng C, Breslow E, Wang BC, Protein Sci. 2001 Sep;10(9):1869-80. PMID:11514677
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