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| - | [[Image:1huw.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1huw| PDB=1huw | SCENE= }} | | {{STRUCTURE_1huw| PDB=1huw | SCENE= }} |
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| - | '''THE CRYSTAL STRUCTURE OF AFFINITY-MATURED HUMAN GROWTH HORMONE AT 2 ANGSTROMS RESOLUTION'''
| + | ===THE CRYSTAL STRUCTURE OF AFFINITY-MATURED HUMAN GROWTH HORMONE AT 2 ANGSTROMS RESOLUTION=== |
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| - | ==Overview==
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| - | A variant of human growth hormone (hGH), in which 15 mutations were introduced with phage display mutagenesis to improve receptor binding affinity by 400-fold, yielded two related crystal forms diffracting to high resolution. The structure of this variant was determined in both crystal forms, one at 2.0 A resolution and one at 2.4 A resolution, using molecular replacement with wild-type hGH taken from the receptor complex structure as a search model. Crystallographic refinement of the 2 A structure gave an R-value R-value of 18.5% for data in the resolution range 8 to 2 A. The final model consists of residues 1 to 128 and 155 to 191, with three side-chains modeled in alternative conformations, together with 77 water molecules. Comparison of the structure with wild-type hGH shows that most of the secondary structural elements are unchanged. The exception is the first turn of the third helix in the four-helix bundle core, which is unraveled in the present variant. Analysis of the two related packing environments suggests that this change is caused by crystal packing forces. A large change in the orientation of a short segment of helix found in the connection between the first two core helices is interpreted as evidence for rigid-body variability of this helical segment. Analysis of the mutations in light of the structure of the wild-type hGH/receptor complex shows that six of the mutations are buried in the hormone, whereas the remaining nine involve residues that interact with the receptor in the complex.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8107110}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8107110 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8107110}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Vos, A M.De.]] | | [[Category: Vos, A M.De.]] |
| | [[Category: Hormone]] | | [[Category: Hormone]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:15:18 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:46:27 2008'' |
Revision as of 05:46, 1 July 2008
Template:STRUCTURE 1huw
THE CRYSTAL STRUCTURE OF AFFINITY-MATURED HUMAN GROWTH HORMONE AT 2 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 8107110
About this Structure
1HUW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of affinity-matured human growth hormone at 2 A resolution., Ultsch MH, Somers W, Kossiakoff AA, de Vos AM, J Mol Biol. 1994 Feb 11;236(1):286-99. PMID:8107110
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