From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1gzy.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1gzy.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1gzy| PDB=1gzy | SCENE= }} | | {{STRUCTURE_1gzy| PDB=1gzy | SCENE= }} |
| | | | |
| - | '''HUMAN INSULIN-LIKE GROWTH FACTOR; IN-HOUSE DATA'''
| + | ===HUMAN INSULIN-LIKE GROWTH FACTOR; IN-HOUSE DATA=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Human insulin-like growth factors I and II (hIGF-I, hIGF-II) are potent stimulators of cell and growth processes. They display high sequence similarity to both the A and B chains of insulin but contain an additional connecting C-domain, which reflects their secretion without specific packaging or precursor conversion. IGFs also have an extension at the C-terminus known as the D-domain. This paper describes four homologous hIGF-1 structures, obtained from crystals grown in the presence of the detergent SB12, which reveal additional detail in the C- and D-domains. Two different detergent binding modes observed in the crystals may reflect different hIGF-I biological properties such as the interaction with IGF binding proteins and self-aggregation. While the helical core of hIGF-I is very similar to that in insulin, there are distinct differences in the region of hIGF-I corresponding to the insulin B chain C-terminus, residues B25-B30. In hIGF-I, these residues (24-29) and the following C-domain form an extensive loop protruding 20 A from the core, which results in a substantially different conformation for the receptor binding epitope in hIGF-I compared to insulin. One notable feature of the structures presented here is demonstration of peptide-bond cleavage between Ser35 and Arg36 resulting in an apparent gap between residues 35 and 39. The equivalent region of proinsulin is involved in hormone processing demanding a reassessment of the structural integrity of hIGF-I in relation to its biological function.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12135360}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12135360 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_12135360}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 34: |
Line 38: |
| | [[Category: Insulin family]] | | [[Category: Insulin family]] |
| | [[Category: Plasma]] | | [[Category: Plasma]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:14:06 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:23:28 2008'' |
Revision as of 03:23, 1 July 2008
Template:STRUCTURE 1gzy
HUMAN INSULIN-LIKE GROWTH FACTOR; IN-HOUSE DATA
Template:ABSTRACT PUBMED 12135360
About this Structure
1GZY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural origins of the functional divergence of human insulin-like growth factor-I and insulin., Brzozowski AM, Dodson EJ, Dodson GG, Murshudov GN, Verma C, Turkenburg JP, de Bree FM, Dauter Z, Biochemistry. 2002 Jul 30;41(30):9389-97. PMID:12135360
Page seeded by OCA on Tue Jul 1 06:23:28 2008
