6rlx

X-RAY STRUCTURE OF HUMAN RELAXIN AT 1.5 ANGSTROMS. COMPARISON TO INSULIN AND IMPLICATIONS FOR RECEPTOR BINDING DETERMINANTS

spinqualitylabelsall models 6rlx, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rlx is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: PCA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [REL2_HUMAN] Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. May be involved in remodeling of connective tissues during pregnancy, promoting growth of pubic ligaments and ripening of the cervix. Publication Abstract from PubMed The X-ray crystal structure of relaxin at 1.5 A resolution is reported for the physiologically active form of the human hormone. Relaxin is a small, two-chain polypeptide that is a member of the protein hormone family that also includes insulin and the insulin-like growth factors IGF-I and IGF-II. These hormones have biologically diverse activities but are structurally similar, sharing a distinctive pattern of cysteine and glycine residues. The predicted structural homology of relaxin to insulin is confirmed by this structural analysis; however, there are significant differences in the terminal regions of the b-chain. Although relaxin, like insulin, crystallizes as a dimer, the orientation of the molecules in the respective dimers is completely different. The region of the relaxin molecule proposed to be involved in receptor binding is part of the dimer interface, suggesting that some of the other residues contained in the dimer contact surface might be receptor binding determinants as well. The proposed receptor binding determinants for insulin likewise include residues at its dimer interface. However, because the dimer contacts of relaxin and insulin are quite different, it appears that these two structurally related hormones have evolved somewhat dissimilar mechanisms for receptor binding. X-ray structure of human relaxin at 1.5 A. Comparison to insulin and implications for receptor binding determinants.,Eigenbrot C, Randal M, Quan C, Burnier J, O'Connell L, Rinderknecht E, Kossiakoff AA J Mol Biol. 1991 Sep 5;221(1):15-21. PMID:1656049 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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