Identification of Hot spots in Sm protein interfaces
Конференцијски прилог (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
This study aims to characterize the interface hot spot
residues of subunits in Sm proteins. We performed an analysis of the X ray structure of 15 Sm
motif containing proteins from the Protein Data Bank (PDB) and summarize physicochemical
properties in an effort to understand the origin of their stabilizing contributions to protein–
protein associations.Our results show that low relCompASA is critical for a residue to be a hot spot. Though
many of the hot spot residues have similar relCompASA values with nonhot spot residues,
they have different mean values (hot spots: 5.1%, non-hot spots: 29.1%). The P-value for
relCompASA is less than 0.05, which indicate that hot spots located near the center of the
interface are a general property of the interfaces, and largely protected from bulk solvent
(corresponding to low relCompASA). RelDASA indicates the change in the solvent
accessibility of a residue, and correlate significantly with relCompASA. Additionally,
knowledge-based pair... potentials of residues is statistically significant to discriminate hot
spots and non-hot spots (P-value = 5.7×10−6). These results indicate that hot spots are mostly
buried, tightly packed and form a network of favorable interactions with other residues.
Structurally conserved residues and hot spots correlate significantly, and demonstrate
that hot spots play an important role in the stability of oligomers.
Кључне речи:
Hot spots / Sm family of proteins / Protein Data BankИзвор:
Book of abstracts - Second Humboldt conference on noncovalent interactions, October 22-25, 2009, Vršac, Serbia, 2009, 75-75Издавач:
- Belgrade, Serbia : Faculty of Chemistry, University of Belgrade
- Germany : Alexander von Humboldt Foundation
Финансирање / пројекти:
- Проучавање односа реактивности, нековалентних интеракција и структуре молекула и моделовање хемијских система (RS-MESTD-MPN2006-2010-142037)
- Аутоматско резоновање и напредне обраде великих количина података и текста (RS-MESTD-MPN2006-2010-144030)
Институција/група
IHTMTY - CONF AU - Stojanović, Srđan AU - Zarić, Božidarka AU - Zarić, Snežana PY - 2009 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/6531 AB - This study aims to characterize the interface hot spot residues of subunits in Sm proteins. We performed an analysis of the X ray structure of 15 Sm motif containing proteins from the Protein Data Bank (PDB) and summarize physicochemical properties in an effort to understand the origin of their stabilizing contributions to protein– protein associations.Our results show that low relCompASA is critical for a residue to be a hot spot. Though many of the hot spot residues have similar relCompASA values with nonhot spot residues, they have different mean values (hot spots: 5.1%, non-hot spots: 29.1%). The P-value for relCompASA is less than 0.05, which indicate that hot spots located near the center of the interface are a general property of the interfaces, and largely protected from bulk solvent (corresponding to low relCompASA). RelDASA indicates the change in the solvent accessibility of a residue, and correlate significantly with relCompASA. Additionally, knowledge-based pair potentials of residues is statistically significant to discriminate hot spots and non-hot spots (P-value = 5.7×10−6). These results indicate that hot spots are mostly buried, tightly packed and form a network of favorable interactions with other residues. Structurally conserved residues and hot spots correlate significantly, and demonstrate that hot spots play an important role in the stability of oligomers. PB - Belgrade, Serbia : Faculty of Chemistry, University of Belgrade PB - Germany : Alexander von Humboldt Foundation C3 - Book of abstracts - Second Humboldt conference on noncovalent interactions, October 22-25, 2009, Vršac, Serbia T1 - Identification of Hot spots in Sm protein interfaces SP - 75 EP - 75 UR - https://hdl.handle.net/21.15107/rcub_cer_6531 ER -
@conference{ author = "Stojanović, Srđan and Zarić, Božidarka and Zarić, Snežana", year = "2009", abstract = "This study aims to characterize the interface hot spot residues of subunits in Sm proteins. We performed an analysis of the X ray structure of 15 Sm motif containing proteins from the Protein Data Bank (PDB) and summarize physicochemical properties in an effort to understand the origin of their stabilizing contributions to protein– protein associations.Our results show that low relCompASA is critical for a residue to be a hot spot. Though many of the hot spot residues have similar relCompASA values with nonhot spot residues, they have different mean values (hot spots: 5.1%, non-hot spots: 29.1%). The P-value for relCompASA is less than 0.05, which indicate that hot spots located near the center of the interface are a general property of the interfaces, and largely protected from bulk solvent (corresponding to low relCompASA). RelDASA indicates the change in the solvent accessibility of a residue, and correlate significantly with relCompASA. Additionally, knowledge-based pair potentials of residues is statistically significant to discriminate hot spots and non-hot spots (P-value = 5.7×10−6). These results indicate that hot spots are mostly buried, tightly packed and form a network of favorable interactions with other residues. Structurally conserved residues and hot spots correlate significantly, and demonstrate that hot spots play an important role in the stability of oligomers.", publisher = "Belgrade, Serbia : Faculty of Chemistry, University of Belgrade, Germany : Alexander von Humboldt Foundation", journal = "Book of abstracts - Second Humboldt conference on noncovalent interactions, October 22-25, 2009, Vršac, Serbia", title = "Identification of Hot spots in Sm protein interfaces", pages = "75-75", url = "https://hdl.handle.net/21.15107/rcub_cer_6531" }
Stojanović, S., Zarić, B.,& Zarić, S.. (2009). Identification of Hot spots in Sm protein interfaces. in Book of abstracts - Second Humboldt conference on noncovalent interactions, October 22-25, 2009, Vršac, Serbia Belgrade, Serbia : Faculty of Chemistry, University of Belgrade., 75-75. https://hdl.handle.net/21.15107/rcub_cer_6531
Stojanović S, Zarić B, Zarić S. Identification of Hot spots in Sm protein interfaces. in Book of abstracts - Second Humboldt conference on noncovalent interactions, October 22-25, 2009, Vršac, Serbia. 2009;:75-75. https://hdl.handle.net/21.15107/rcub_cer_6531 .
Stojanović, Srđan, Zarić, Božidarka, Zarić, Snežana, "Identification of Hot spots in Sm protein interfaces" in Book of abstracts - Second Humboldt conference on noncovalent interactions, October 22-25, 2009, Vršac, Serbia (2009):75-75, https://hdl.handle.net/21.15107/rcub_cer_6531 .