6rlx
From Proteopedia
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| - | [[Image:6rlx.gif|left|200px]] | + | [[Image:6rlx.gif|left|200px]] |
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| - | '''X-RAY STRUCTURE OF HUMAN RELAXIN AT 1.5 ANGSTROMS. COMPARISON TO INSULIN AND IMPLICATIONS FOR RECEPTOR BINDING DETERMINANTS''' | + | {{Structure |
| + | |PDB= 6rlx |SIZE=350|CAPTION= <scene name='initialview01'>6rlx</scene>, resolution 1.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''X-RAY STRUCTURE OF HUMAN RELAXIN AT 1.5 ANGSTROMS. COMPARISON TO INSULIN AND IMPLICATIONS FOR RECEPTOR BINDING DETERMINANTS''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 6RLX is a [ | + | 6RLX is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RLX OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1656049 1656049] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: hormone(muscle relaxant)]] | [[Category: hormone(muscle relaxant)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:14:01 2008'' |
Revision as of 17:14, 20 March 2008
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X-RAY STRUCTURE OF HUMAN RELAXIN AT 1.5 ANGSTROMS. COMPARISON TO INSULIN AND IMPLICATIONS FOR RECEPTOR BINDING DETERMINANTS
Overview
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.
About this Structure
6RLX is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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