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A C-terminal segment of the V1R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein.
Adikesavan, Nallini Vijayarangan; Mahmood, Syed Saad; Stanley, Nithianantham; Xu, Zhen; Wu, Nan; Thibonnier, Marc; Shoham, Menachem.
Affiliation
  • Adikesavan NV; Department of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, OH 44106-4935, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun ; 61(Pt 4): 341-5, 2005 Apr 01.
Article in En | MEDLINE | ID: mdl-16511036
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peptide Fragments / Carrier Proteins / Receptors, Vasopressin Limits: Humans Language: En Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Year: 2005 Document type: Article Affiliation country: United States Country of publication: United kingdom
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peptide Fragments / Carrier Proteins / Receptors, Vasopressin Limits: Humans Language: En Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Year: 2005 Document type: Article Affiliation country: United States Country of publication: United kingdom