1bet
From Proteopedia
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| - | [[Image:1bet.gif|left|200px]] | + | [[Image:1bet.gif|left|200px]] |
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| - | '''NEW PROTEIN FOLD REVEALED BY A 2.3 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF NERVE GROWTH FACTOR''' | + | {{Structure |
| + | |PDB= 1bet |SIZE=350|CAPTION= <scene name='initialview01'>1bet</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''NEW PROTEIN FOLD REVEALED BY A 2.3 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF NERVE GROWTH FACTOR''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BET is a [ | + | 1BET is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. The following page contains interesting information on the relation of 1BET with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb68_1.html Neurotrophins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BET OCA]. |
==Reference== | ==Reference== | ||
| - | New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor., McDonald NQ, Lapatto R, Murray-Rust J, Gunning J, Wlodawer A, Blundell TL, Nature. 1991 Dec 5;354(6352):411-4. PMID:[http:// | + | New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor., McDonald NQ, Lapatto R, Murray-Rust J, Gunning J, Wlodawer A, Blundell TL, Nature. 1991 Dec 5;354(6352):411-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1956407 1956407] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Neurotrophins]] | [[Category: Neurotrophins]] | ||
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[[Category: growth factor]] | [[Category: growth factor]] | ||
| - | ''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 10:10:03 2008'' |
Revision as of 08:10, 20 March 2008
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NEW PROTEIN FOLD REVEALED BY A 2.3 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF NERVE GROWTH FACTOR
Overview
Nerve growth factor (NGF) is a member of an expanding family of neurotrophic factors (including brain-derived neurotrophic factor and the neurotrophins) that control the development and survival of certain neuronal populations both in the peripheral and in the central nervous systems. Its biological effects are mediated by a high-affinity ligand-receptor interaction and a tyrosine kinase signalling pathway. A potential use for NGF and its relatives in the treatment of neurological disorders such as Alzheimer's disease and Parkinson's disease requires an understanding of the structure-function relationships of NGF. NGF is a dimeric molecule, with 118 amino acids per protomer. We report the crystal structure of the murine NGF dimer at 2.3-A resolution, which reveals a novel protomer structure consisting of three antiparallel pairs of beta strands, together forming a flat surface. Two subunits associate through this surface, thus burying a total of 2,332 A. Four loop regions, which contain many of the variable residues observed between different NGF-related molecules, may determine the different receptor specificities. A clustering of positively charged side chains may provide a complementary interaction with the acidic low-affinity NGF receptor. The structure provides a model for rational design of analogues of NGF and its relatives and for testing the NGF-receptor recognition determinants critical for signal transduction.
About this Structure
1BET is a Single protein structure of sequence from Mus musculus. The following page contains interesting information on the relation of 1BET with [Neurotrophins]. Full crystallographic information is available from OCA.
Reference
New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor., McDonald NQ, Lapatto R, Murray-Rust J, Gunning J, Wlodawer A, Blundell TL, Nature. 1991 Dec 5;354(6352):411-4. PMID:1956407
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