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A tangible 3D model of the human Adipocyte Plasma Membrane‐Associated Protein (APMAP)
Author(s) -
Colton Shan,
Herman Tim,
Giles Kurt,
Koo Ben,
Jeske Sabine,
Hicks Michael,
DeBella Stan
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.470.1
Subject(s) - homology modeling , computational biology , function (biology) , gene , homology (biology) , threading (protein sequence) , amino acid , biochemistry , biology , chemistry , microbiology and biotechnology , protein structure , enzyme
Though the human genome has been decoded, we still know relatively little about the function of many of our genes and gene products. One such example is the human protein encoded by chromosome 20, open reading frame 3, also known as adipocyte plasma membrane‐associated protein (APMAP). The functionally characterized protein to which APMAP shares the highest level of amino acid similarity is the plant protein strictosidine synthase, which functions as the precursor to the medically relevant indole alkaloid biosynthesis pathway. However, orthogonal sources of information suggest APMAP may function quite differently. Protein structure can often provide unique insights into molecular function that amino acid sequence alone cannot. Using the homology‐based threading program Modeller (Sali and Blundell. J. Mol. Biol. 234, 779–815, 1993.), a reasonable three‐dimensional model of APMAP was generated. Using rapid prototyping technology, we have built tangible 3D models of this protein. The SMART (Students Modeling A Research Topic) program was established by the Center of BioMolecular Modeling at the Milwaukee School of Engineering and involves partnerships between university researchers and local high schools. This work is funded by NIH‐NCRR‐SEPA and HHMI.