1JK6

UNCOMPLEXED DES 1-6 BOVINE NEUROPHYSIN

Summary for 1JK6

• Entry DOI: 10.2210/pdb1jk6/pdb
• Related: 1JK4 1NPO 2bn2
• Descriptor: NEUROPHYSIN 2 (2 entities in total)
• Functional Keywords: neurophysin, hormone transport, hypothalamus, neuropeptide
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted: P01180
• Total number of polymer chains: 2
• Total formula weight: 18487.08

Authors

Rose, J.P.,Wang, B.-C. (deposition date: 2001-07-11, release date: 2003-04-29, Last modification date: 2024-11-06)

Primary citation

Wu, C.K.,Hu, B.,Rose, J.P.,Liu, Z.J.,Nguyen, T.L.,Zeng, C.,Breslow, E.,Wang, B.C.
Structures of an Unliganded Neurophysin and its Vasopressin Complex: Implications for Binding and Allosteric Mechanisms
Protein Sci., 10:1869-1880, 2003

PubMed Abstract: 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.

PubMed: 11514677
DOI: 10.1110/ps.10601

Experimental method

X-RAY DIFFRACTION (2.4 Å)