1h02: Difference between revisions

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[[Image:1h02.gif|left|200px]]<br /><applet load="1h02" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1h02.gif|left|200px]]
caption="1h02, resolution 2.00&Aring;" />
 
'''HUMAN INSULIN-LIKE GROWTH FACTOR; SRS DARESBURY DATA'''<br />
{{Structure
|PDB= 1h02 |SIZE=350|CAPTION= <scene name='initialview01'>1h02</scene>, resolution 2.00&Aring;
|SITE= <scene name='pdbsite=C15:C15+Binding+Site+For+Chain+B'>C15</scene>
|LIGAND= <scene name='pdbligand=C15:N-DODECYL-N,N-DIMETHYL-3-AMMONIO-1-PROPANESULFONATE'>C15</scene>
|ACTIVITY=
|GENE=
}}
 
'''HUMAN INSULIN-LIKE GROWTH FACTOR; SRS DARESBURY DATA'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1H02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=C15:'>C15</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1H02 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb52_1.html Growth Hormone]]. Known structural/functional Site: <scene name='pdbsite=C15:C15+Binding+Site+For+Chain+B'>C15</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H02 OCA].  
1H02 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1H02 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb52_1.html Growth Hormone]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H02 OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12135360 12135360]
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:[http://www.ncbi.nlm.nih.gov/pubmed/12135360 12135360]
[[Category: Growth Hormone]]
[[Category: Growth Hormone]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: plasma]]
[[Category: plasma]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:57 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:30:23 2008''

Revision as of 12:30, 20 March 2008

File:1h02.gif


PDB ID 1h02

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, resolution 2.00Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



HUMAN INSULIN-LIKE GROWTH FACTOR; SRS DARESBURY DATA


OverviewOverview

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.

DiseaseDisease

Known disease associated with this structure: Growth retardation with deafness and mental retardation due to IGF1 deficiency OMIM:[147440]

About this StructureAbout this Structure

1H02 is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1H02 with [Growth Hormone]. Full crystallographic information is available from OCA.

ReferenceReference

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

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