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| - | [[Image:1tgr.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1tgr| PDB=1tgr | SCENE= }} | | {{STRUCTURE_1tgr| PDB=1tgr | SCENE= }} |
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| - | '''Crystal Structure of mini-IGF-1(2)'''
| + | ===Crystal Structure of mini-IGF-1(2)=== |
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| - | ==Overview==
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| - | Insulin and insulin-like growth factor 1 (IGF-1) share a homologous sequence, a similar three-dimensional structure and weakly overlapping biological activity, but IGF-1 folds into two thermodynamically stable disulfide isomers, while insulin folds into one unique stable tertiary structure. This is a very interesting phenomenon in which one amino acid sequence encodes two three-dimensional structures, and its molecular mechanism has remained unclear for a long time. In this study, the crystal structure of mini-IGF-1(2), a disulfide isomer of an artificial analog of IGF-1, was solved by the SAD/SIRAS method using our in-house X-ray source. Evidence was found in the structure showing that the intra-A-chain/domain disulfide bond of some molecules was broken; thus, it was proposed that disulfide isomerization begins with the breakdown of this disulfide bond. Furthermore, based on the structural comparison of IGF-1 and insulin, a new assumption was made that in insulin the several hydrogen bonds formed between the N-terminal region of the B-chain and the intra-A-chain disulfide region of the A-chain are the main reason for the stability of the intra-A-chain disulfide bond and for the prevention of disulfide isomerization, while Phe B1 and His B5 are very important for the formation of these hydrogen bonds. Moreover, the receptor binding property of IGF-1 was analyzed in detail based on the structural comparison of mini-IGF-1(2), native IGF-1, and small mini-IGF-1.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15567151}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15567151 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15567151}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Igf-i]] | | [[Category: Igf-i]] |
| | [[Category: Recepter binding]] | | [[Category: Recepter binding]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:55:48 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:33:42 2008'' |
Revision as of 10:33, 28 July 2008
Template:STRUCTURE 1tgr
Crystal Structure of mini-IGF-1(2)
Template:ABSTRACT PUBMED 15567151
About this Structure
1TGR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
1.42A crystal structure of mini-IGF-1(2): an analysis of the disulfide isomerization property and receptor binding property of IGF-1 based on the three-dimensional structure., Yun CH, Tang YH, Feng YM, An XM, Chang WR, Liang DC, Biochem Biophys Res Commun. 2005 Jan 7;326(1):52-9. PMID:15567151
Page seeded by OCA on Mon Jul 28 13:33:42 2008
