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| | {{STRUCTURE_2hnv| PDB=2hnv | SCENE= }} | | {{STRUCTURE_2hnv| PDB=2hnv | SCENE= }} |
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| - | '''Crystal Structure of a Dipeptide Complex of the Q58V Mutant of Bovine Neurophysin-I'''
| + | ===Crystal Structure of a Dipeptide Complex of the Q58V Mutant of Bovine Neurophysin-I=== |
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| - | ==Overview==
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| - | Current evidence indicates that the ligand-facilitated dimerization of neurophysin is mediated in part by dimerization-induced changes at the hormone binding site of the unliganded state that increase ligand affinity. To elucidate other contributory factors, we investigated the potential role of neurophysin's short interdomain loop (residues 55-59), particularly the effects of loop residue mutation and of deleting amino-terminal residues 1-6, which interact with the loop and adjacent residues 53-54. The neurophysin studied was bovine neurophysin-I, necessitating determination of the crystal structures of des 1-6 bovine neurophysin-I in unliganded and liganded dimeric states, as well as the structure of its liganded Q58V mutant, in which peptide was bound with unexpectedly increased affinity. Increases in dimerization constant associated with selected loop residue mutations and with deletion of residues 1-6, together with structural data, provided evidence that dimerization of unliganded neurophysin-I is constrained by hydrogen bonding of the side chains of Gln58, Ser56, and Gln55 and by amino terminus interactions, loss or alteration of these hydrogen bonds, and probable loss of amino terminus interactions, contributing to the increased dimerization of the liganded state. An additional intersubunit hydrogen bond from residue 81, present only in the liganded state, was demonstrated as the largest single effect of ligand binding directly on the subunit interface. Comparison of bovine neurophysins I and II indicates broadly similar mechanisms for both, with the exception in neurophysin II of the absence of Gln55 side chain hydrogen bonds in the unliganded state and a more firmly established loss of amino terminus interactions in the liganded state. Evidence is presented that loop status modulates dimerization via long-range effects on neurophysin conformation involving neighboring Phe22 as a key intermediary.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17192588}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17192588 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17192588}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Protein-pepide complex]] | | [[Category: Protein-pepide complex]] |
| | [[Category: Q58v mutant]] | | [[Category: Q58v mutant]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:29:56 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:56:59 2008'' |
Revision as of 12:57, 29 July 2008
Template:STRUCTURE 2hnv
Crystal Structure of a Dipeptide Complex of the Q58V Mutant of Bovine Neurophysin-I
Template:ABSTRACT PUBMED 17192588
About this Structure
2HNV is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Contributions of the interdomain loop, amino terminus, and subunit interface to the ligand-facilitated dimerization of neurophysin: crystal structures and mutation studies of bovine neurophysin-I., Li X, Lee H, Wu J, Breslow E, Protein Sci. 2007 Jan;16(1):52-68. PMID:17192588
Page seeded by OCA on Tue Jul 29 15:56:59 2008
