Bezerra, Katyanna Sales2017-01-232017-01-232016-03-18BEZERRA, Katyanna Sales. Análise in silico da interação entre a integrina α2β1 e o colágeno. 2016. 97f. Dissertação (Mestrado em Ciências Biológicas) - Centro de Biociências, Universidade Federal do Rio Grande do Norte, Natal, 2016.https://repositorio.ufrn.br/jspui/handle/123456789/21718The extracellular matrix (ECM) of connective tissues is a complex of many members of several families of proteins that delineate its structural integrity and various physiological functions. The interactions occurring between the matrix cell and play a key role in cell attachment and migration, as well as regulate and promote cell differentiation and gene expression. The control of these cellular interactions is determinative for most biological processes. Integrins are a family of transmembrane glycoproteins that function as the main metazoan receptors for cell adhesion plays a central role in a physical support functions for signal transduction, cytoskeletal actin assembly, gene expression and cell functions. These glycoproteins may bind to the extracellular matrix glycoproteins such as collagen, this connection allows adjustment and integrity of cell adhesion, cell migration and immune response. Thus, this study aims to perform an ab initio analysis of the interaction between the domain-I integrin α2β1 and collagen with GFOGER sequence. The analysis was carried out using quantum mechanical calculations within Density Functional Theory (DFT) with the Generalized Gradient Approximation (GGA) for describing the exchange and correlation effects. The energies of interaction between domain-I α2 integrin residues and collagen residues were calculated using the Molecular Fragmentation with Conjugated Caps (MFCC). The results demonstrate the importance of metal ion present in the MIDAS region of the integrin for interaction with the collagen molecule. The analysis showed the interaction energies residues Arg12, Glu33, Arg34, Glu55, and Arg56 GFOGER sequence of collagen, as important to the interaction with the integrin. In the residues of integrin shown to be of great relevance to the interaction were Thr221, Asp219, Asp254 and Glu256. Moreover, the results also highlight the importance of changing the conformation of these residues during the interaction between the proteins. These results can aid understanding of events involving the interaction between integrin α2β1 and collagen as well as provide relevant data on special aspects presented in mutations models.Acesso AbertoIntegrinaColágenoEnergia de interaçãoDFTmasterThesisCNPQ::CIENCIAS BIOLOGICAS