1ang
From Proteopedia
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| - | [[Image:1ang.jpg|left|200px]] | + | [[Image:1ang.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN REVEALS THE STRUCTURAL BASIS FOR ITS FUNCTIONAL DIVERGENCE FROM RIBONUCLEASE''' | + | {{Structure |
| + | |PDB= 1ang |SIZE=350|CAPTION= <scene name='initialview01'>1ang</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN REVEALS THE STRUCTURAL BASIS FOR ITS FUNCTIONAL DIVERGENCE FROM RIBONUCLEASE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ANG is a [ | + | 1ANG is a [[Single protein]] structure of sequence 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=1ANG OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease., Acharya KR, Shapiro R, Allen SC, Riordan JF, Vallee BL, Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):2915-9. PMID:[http:// | + | Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease., Acharya KR, Shapiro R, Allen SC, Riordan JF, Vallee BL, Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):2915-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8159679 8159679] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase (vascularization)]] | [[Category: hydrolase (vascularization)]] | ||
| - | ''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 09:59:56 2008'' |
Revision as of 07:59, 20 March 2008
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CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN REVEALS THE STRUCTURAL BASIS FOR ITS FUNCTIONAL DIVERGENCE FROM RIBONUCLEASE
Contents |
Overview
Angiogenin, a potent inducer of neovascularization, is the only angiogenic molecule known to exhibit ribonucleolytic activity. Its overall structure, as determined at 2.4 A, is similar to that of pancreatic ribonuclease A, but it differs markedly in several distinct areas, particularly the ribonucleolytic active center and the putative receptor binding site, both of which are critically involved in biological function. Most strikingly, the site that is spatially analogous to that for pyrimidine binding in ribonuclease A differs significantly in conformation and is "obstructed" by glutamine-117. Movement of this and adjacent residues may be required for substrate binding to angiogenin and, hence, constitute a key part of its mechanism of action.
Disease
Known diseases associated with this structure: Amyotrophic lateral sclerosis, susceptibility to OMIM:[105850]
About this Structure
1ANG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease., Acharya KR, Shapiro R, Allen SC, Riordan JF, Vallee BL, Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):2915-9. PMID:8159679
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