1XY8
NMR strcutre of sst1-selective somatostatin (SRIF) analog 1
Summary for 1XY8
| Entry DOI | 10.2210/pdb1xy8/pdb |
| Related | 1XXZ 1XY4 1XY5 1XY6 1XY9 |
| NMR Information | BMRB: 6425 |
| Descriptor | SST1-selective somatosatin analog (1 entity in total) |
| Functional Keywords | gamma turn, hormone-growth factor complex, hormone/growth factor |
| Total number of polymer chains | 1 |
| Total formula weight | 1689.03 |
| Authors | Grace, C.R.R.,Durrer, L.,Koerber, S.C.,Erchegyi, J.,Reubi, J.C.,Rivier, J.E.,Riek, R. (deposition date: 2004-11-09, release date: 2005-02-15, Last modification date: 2022-03-02) |
| Primary citation | Grace, C.R.R.,Durrer, L.,Koerber, S.C.,Erchegyi, J.,Reubi, J.C.,Rivier, J.E.,Riek, R. Somatostatin receptor 1 selective analogues: 4. Three-dimensional consensus structure by NMR J.Med.Chem., 48:523-533, 2005 Cited by PubMed Abstract: The three-dimensional NMR structures of six analogues of somatostatin (SRIF) are described. These analogues with the amino acid 4-(N-isopropyl)-aminomethylphenylalanine (IAmp) at position 9 exhibit potent and highly selective binding to human SRIF subtype 1 receptors (sst(1)). The conformations reveal that the backbones of these analogues have a hairpin-like structure similar to the sst(2)-subtype-selective analogues. This structure serves as a scaffold for retaining a unique arrangement of the side chains of d-Trp(8), IAmp(9), Phe(7), and Phe(11) or m-I-Tyr(11) (m-I-Tyr = mono-iodo-tyrosine). The conformational preferences and results from biological analyses of these analogues(1,2) allow a detailed study of the structure-activity relationship of SRIF. The proposed consensus pharmacophore of the sst(1)-selective analogues requires a unique set of distances between an indole/2-naphthyl ring, an IAmp side chain, and two aromatic rings. This motif is necessary and sufficient to explain the binding affinities of all of the analogues studied and is distinct from the existing models suggested for sst(4) as well as sst(2)/sst(5) selectivity. PubMed: 15658866DOI: 10.1021/jm049518u PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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